Conformational analysis of the blue-light sensing protein YtvA reveals a competitive interface for LOV—LOV dimerization and interdomain interactions
Abstract The Bacillus subtilis protein YtvA is related to plant phototropins in that it senses UVA—blue-light by means of the flavin binding LOV domain, linked to a nucleotide-binding STAS domain. The structural basis for interdomain interactions and functional regulation are not known. Here we repo...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Buttani, Valentina [verfasserIn] Losi, Aba [verfasserIn] Eggert, Thorsten [verfasserIn] Krauss, Ulrich [verfasserIn] Jaeger, Karl-Erich [verfasserIn] Cao, Zhen [verfasserIn] Gärtner, Wolfgang [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2007 |
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| Anmerkung: |
© The Royal Society of Chemistry and Owner Societies 2007 |
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| Übergeordnetes Werk: |
Enthalten in: Photochemical & photobiological sciences - Heidelberg : Springer, 2002, 6(2007), 1 vom: 01. Jan., Seite 41-49 |
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| Übergeordnetes Werk: |
volume:6 ; year:2007 ; number:1 ; day:01 ; month:01 ; pages:41-49 |
| Links: |
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| DOI / URN: |
10.1039/b610375h |
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| Katalog-ID: |
SPR045043817 |
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| 100 | 1 | |a Buttani, Valentina |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Conformational analysis of the blue-light sensing protein YtvA reveals a competitive interface for LOV—LOV dimerization and interdomain interactions |
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| 520 | |a Abstract The Bacillus subtilis protein YtvA is related to plant phototropins in that it senses UVA—blue-light by means of the flavin binding LOV domain, linked to a nucleotide-binding STAS domain. The structural basis for interdomain interactions and functional regulation are not known. Here we report the conformational analysis of three YtvA constructs, by means of size exclusion chromatography, circular dichroism (CD) and molecular docking simulations. The isolated YtvA-LOV domain (YLOV, aa 25–126) has a strong tendency to dimerize, prevented in full-length YtvA, but still observed in YLOV carrying the N-terminal extension (N-YLOV, aa 1–126). The analysis of CD data shows that both the N-terminal cap and the linker region (aa 127–147) between the LOV and the STAS domain are helical and that the central β-scaffold is distorted in the LOV domains dimers. The involvement of the central β-scaffold in dimerization is supported by docking simulation of the YLOV dimer and the importance of this region is highlighted by light-induced conformational changes, emerging from the CD data analysis. In YtvA, the β-strand fraction is notably less distorted and distinct light-driven changes in the loops/turn fraction are detected. The data uncover a common surface for LOV–LOV and intraprotein interaction, involving the central β-scaffold, and offer hints to investigate the molecular basis of light-activation and regulation in LOV proteins. | ||
| 700 | 1 | |a Losi, Aba |e verfasserin |4 aut | |
| 700 | 1 | |a Eggert, Thorsten |e verfasserin |4 aut | |
| 700 | 1 | |a Krauss, Ulrich |e verfasserin |4 aut | |
| 700 | 1 | |a Jaeger, Karl-Erich |e verfasserin |4 aut | |
| 700 | 1 | |a Cao, Zhen |e verfasserin |4 aut | |
| 700 | 1 | |a Gärtner, Wolfgang |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Photochemical & photobiological sciences |d Heidelberg : Springer, 2002 |g 6(2007), 1 vom: 01. Jan., Seite 41-49 |w (DE-627)342893742 |w (DE-600)2072584-X |x 1474-9092 |7 nnns |
| 773 | 1 | 8 | |g volume:6 |g year:2007 |g number:1 |g day:01 |g month:01 |g pages:41-49 |
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10.1039/b610375h doi (DE-627)SPR045043817 (SPR)b610375h-e DE-627 ger DE-627 rakwb eng 620 ASE 35.16 bkl 42.14 bkl Buttani, Valentina verfasserin aut Conformational analysis of the blue-light sensing protein YtvA reveals a competitive interface for LOV—LOV dimerization and interdomain interactions 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Royal Society of Chemistry and Owner Societies 2007 Abstract The Bacillus subtilis protein YtvA is related to plant phototropins in that it senses UVA—blue-light by means of the flavin binding LOV domain, linked to a nucleotide-binding STAS domain. The structural basis for interdomain interactions and functional regulation are not known. Here we report the conformational analysis of three YtvA constructs, by means of size exclusion chromatography, circular dichroism (CD) and molecular docking simulations. The isolated YtvA-LOV domain (YLOV, aa 25–126) has a strong tendency to dimerize, prevented in full-length YtvA, but still observed in YLOV carrying the N-terminal extension (N-YLOV, aa 1–126). The analysis of CD data shows that both the N-terminal cap and the linker region (aa 127–147) between the LOV and the STAS domain are helical and that the central β-scaffold is distorted in the LOV domains dimers. The involvement of the central β-scaffold in dimerization is supported by docking simulation of the YLOV dimer and the importance of this region is highlighted by light-induced conformational changes, emerging from the CD data analysis. In YtvA, the β-strand fraction is notably less distorted and distinct light-driven changes in the loops/turn fraction are detected. The data uncover a common surface for LOV–LOV and intraprotein interaction, involving the central β-scaffold, and offer hints to investigate the molecular basis of light-activation and regulation in LOV proteins. Losi, Aba verfasserin aut Eggert, Thorsten verfasserin aut Krauss, Ulrich verfasserin aut Jaeger, Karl-Erich verfasserin aut Cao, Zhen verfasserin aut Gärtner, Wolfgang verfasserin aut Enthalten in Photochemical & photobiological sciences Heidelberg : Springer, 2002 6(2007), 1 vom: 01. Jan., Seite 41-49 (DE-627)342893742 (DE-600)2072584-X 1474-9092 nnns volume:6 year:2007 number:1 day:01 month:01 pages:41-49 https://dx.doi.org/10.1039/b610375h lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_121 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_374 GBV_ILN_602 GBV_ILN_647 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2093 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2472 GBV_ILN_2522 GBV_ILN_2812 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4346 GBV_ILN_4367 GBV_ILN_4700 GBV_ILN_4753 35.16 ASE 42.14 ASE AR 6 2007 1 01 01 41-49 |
| spelling |
10.1039/b610375h doi (DE-627)SPR045043817 (SPR)b610375h-e DE-627 ger DE-627 rakwb eng 620 ASE 35.16 bkl 42.14 bkl Buttani, Valentina verfasserin aut Conformational analysis of the blue-light sensing protein YtvA reveals a competitive interface for LOV—LOV dimerization and interdomain interactions 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Royal Society of Chemistry and Owner Societies 2007 Abstract The Bacillus subtilis protein YtvA is related to plant phototropins in that it senses UVA—blue-light by means of the flavin binding LOV domain, linked to a nucleotide-binding STAS domain. The structural basis for interdomain interactions and functional regulation are not known. Here we report the conformational analysis of three YtvA constructs, by means of size exclusion chromatography, circular dichroism (CD) and molecular docking simulations. The isolated YtvA-LOV domain (YLOV, aa 25–126) has a strong tendency to dimerize, prevented in full-length YtvA, but still observed in YLOV carrying the N-terminal extension (N-YLOV, aa 1–126). The analysis of CD data shows that both the N-terminal cap and the linker region (aa 127–147) between the LOV and the STAS domain are helical and that the central β-scaffold is distorted in the LOV domains dimers. The involvement of the central β-scaffold in dimerization is supported by docking simulation of the YLOV dimer and the importance of this region is highlighted by light-induced conformational changes, emerging from the CD data analysis. In YtvA, the β-strand fraction is notably less distorted and distinct light-driven changes in the loops/turn fraction are detected. The data uncover a common surface for LOV–LOV and intraprotein interaction, involving the central β-scaffold, and offer hints to investigate the molecular basis of light-activation and regulation in LOV proteins. Losi, Aba verfasserin aut Eggert, Thorsten verfasserin aut Krauss, Ulrich verfasserin aut Jaeger, Karl-Erich verfasserin aut Cao, Zhen verfasserin aut Gärtner, Wolfgang verfasserin aut Enthalten in Photochemical & photobiological sciences Heidelberg : Springer, 2002 6(2007), 1 vom: 01. Jan., Seite 41-49 (DE-627)342893742 (DE-600)2072584-X 1474-9092 nnns volume:6 year:2007 number:1 day:01 month:01 pages:41-49 https://dx.doi.org/10.1039/b610375h lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_121 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_374 GBV_ILN_602 GBV_ILN_647 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2093 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2472 GBV_ILN_2522 GBV_ILN_2812 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4346 GBV_ILN_4367 GBV_ILN_4700 GBV_ILN_4753 35.16 ASE 42.14 ASE AR 6 2007 1 01 01 41-49 |
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10.1039/b610375h doi (DE-627)SPR045043817 (SPR)b610375h-e DE-627 ger DE-627 rakwb eng 620 ASE 35.16 bkl 42.14 bkl Buttani, Valentina verfasserin aut Conformational analysis of the blue-light sensing protein YtvA reveals a competitive interface for LOV—LOV dimerization and interdomain interactions 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Royal Society of Chemistry and Owner Societies 2007 Abstract The Bacillus subtilis protein YtvA is related to plant phototropins in that it senses UVA—blue-light by means of the flavin binding LOV domain, linked to a nucleotide-binding STAS domain. The structural basis for interdomain interactions and functional regulation are not known. Here we report the conformational analysis of three YtvA constructs, by means of size exclusion chromatography, circular dichroism (CD) and molecular docking simulations. The isolated YtvA-LOV domain (YLOV, aa 25–126) has a strong tendency to dimerize, prevented in full-length YtvA, but still observed in YLOV carrying the N-terminal extension (N-YLOV, aa 1–126). The analysis of CD data shows that both the N-terminal cap and the linker region (aa 127–147) between the LOV and the STAS domain are helical and that the central β-scaffold is distorted in the LOV domains dimers. The involvement of the central β-scaffold in dimerization is supported by docking simulation of the YLOV dimer and the importance of this region is highlighted by light-induced conformational changes, emerging from the CD data analysis. In YtvA, the β-strand fraction is notably less distorted and distinct light-driven changes in the loops/turn fraction are detected. The data uncover a common surface for LOV–LOV and intraprotein interaction, involving the central β-scaffold, and offer hints to investigate the molecular basis of light-activation and regulation in LOV proteins. Losi, Aba verfasserin aut Eggert, Thorsten verfasserin aut Krauss, Ulrich verfasserin aut Jaeger, Karl-Erich verfasserin aut Cao, Zhen verfasserin aut Gärtner, Wolfgang verfasserin aut Enthalten in Photochemical & photobiological sciences Heidelberg : Springer, 2002 6(2007), 1 vom: 01. Jan., Seite 41-49 (DE-627)342893742 (DE-600)2072584-X 1474-9092 nnns volume:6 year:2007 number:1 day:01 month:01 pages:41-49 https://dx.doi.org/10.1039/b610375h lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_121 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_374 GBV_ILN_602 GBV_ILN_647 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2093 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2472 GBV_ILN_2522 GBV_ILN_2812 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4346 GBV_ILN_4367 GBV_ILN_4700 GBV_ILN_4753 35.16 ASE 42.14 ASE AR 6 2007 1 01 01 41-49 |
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10.1039/b610375h doi (DE-627)SPR045043817 (SPR)b610375h-e DE-627 ger DE-627 rakwb eng 620 ASE 35.16 bkl 42.14 bkl Buttani, Valentina verfasserin aut Conformational analysis of the blue-light sensing protein YtvA reveals a competitive interface for LOV—LOV dimerization and interdomain interactions 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Royal Society of Chemistry and Owner Societies 2007 Abstract The Bacillus subtilis protein YtvA is related to plant phototropins in that it senses UVA—blue-light by means of the flavin binding LOV domain, linked to a nucleotide-binding STAS domain. The structural basis for interdomain interactions and functional regulation are not known. Here we report the conformational analysis of three YtvA constructs, by means of size exclusion chromatography, circular dichroism (CD) and molecular docking simulations. The isolated YtvA-LOV domain (YLOV, aa 25–126) has a strong tendency to dimerize, prevented in full-length YtvA, but still observed in YLOV carrying the N-terminal extension (N-YLOV, aa 1–126). The analysis of CD data shows that both the N-terminal cap and the linker region (aa 127–147) between the LOV and the STAS domain are helical and that the central β-scaffold is distorted in the LOV domains dimers. The involvement of the central β-scaffold in dimerization is supported by docking simulation of the YLOV dimer and the importance of this region is highlighted by light-induced conformational changes, emerging from the CD data analysis. In YtvA, the β-strand fraction is notably less distorted and distinct light-driven changes in the loops/turn fraction are detected. The data uncover a common surface for LOV–LOV and intraprotein interaction, involving the central β-scaffold, and offer hints to investigate the molecular basis of light-activation and regulation in LOV proteins. Losi, Aba verfasserin aut Eggert, Thorsten verfasserin aut Krauss, Ulrich verfasserin aut Jaeger, Karl-Erich verfasserin aut Cao, Zhen verfasserin aut Gärtner, Wolfgang verfasserin aut Enthalten in Photochemical & photobiological sciences Heidelberg : Springer, 2002 6(2007), 1 vom: 01. Jan., Seite 41-49 (DE-627)342893742 (DE-600)2072584-X 1474-9092 nnns volume:6 year:2007 number:1 day:01 month:01 pages:41-49 https://dx.doi.org/10.1039/b610375h lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_121 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_374 GBV_ILN_602 GBV_ILN_647 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2093 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2472 GBV_ILN_2522 GBV_ILN_2812 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4346 GBV_ILN_4367 GBV_ILN_4700 GBV_ILN_4753 35.16 ASE 42.14 ASE AR 6 2007 1 01 01 41-49 |
| allfieldsSound |
10.1039/b610375h doi (DE-627)SPR045043817 (SPR)b610375h-e DE-627 ger DE-627 rakwb eng 620 ASE 35.16 bkl 42.14 bkl Buttani, Valentina verfasserin aut Conformational analysis of the blue-light sensing protein YtvA reveals a competitive interface for LOV—LOV dimerization and interdomain interactions 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Royal Society of Chemistry and Owner Societies 2007 Abstract The Bacillus subtilis protein YtvA is related to plant phototropins in that it senses UVA—blue-light by means of the flavin binding LOV domain, linked to a nucleotide-binding STAS domain. The structural basis for interdomain interactions and functional regulation are not known. Here we report the conformational analysis of three YtvA constructs, by means of size exclusion chromatography, circular dichroism (CD) and molecular docking simulations. The isolated YtvA-LOV domain (YLOV, aa 25–126) has a strong tendency to dimerize, prevented in full-length YtvA, but still observed in YLOV carrying the N-terminal extension (N-YLOV, aa 1–126). The analysis of CD data shows that both the N-terminal cap and the linker region (aa 127–147) between the LOV and the STAS domain are helical and that the central β-scaffold is distorted in the LOV domains dimers. The involvement of the central β-scaffold in dimerization is supported by docking simulation of the YLOV dimer and the importance of this region is highlighted by light-induced conformational changes, emerging from the CD data analysis. In YtvA, the β-strand fraction is notably less distorted and distinct light-driven changes in the loops/turn fraction are detected. The data uncover a common surface for LOV–LOV and intraprotein interaction, involving the central β-scaffold, and offer hints to investigate the molecular basis of light-activation and regulation in LOV proteins. Losi, Aba verfasserin aut Eggert, Thorsten verfasserin aut Krauss, Ulrich verfasserin aut Jaeger, Karl-Erich verfasserin aut Cao, Zhen verfasserin aut Gärtner, Wolfgang verfasserin aut Enthalten in Photochemical & photobiological sciences Heidelberg : Springer, 2002 6(2007), 1 vom: 01. Jan., Seite 41-49 (DE-627)342893742 (DE-600)2072584-X 1474-9092 nnns volume:6 year:2007 number:1 day:01 month:01 pages:41-49 https://dx.doi.org/10.1039/b610375h lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_121 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_374 GBV_ILN_602 GBV_ILN_647 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2093 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2119 GBV_ILN_2129 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2190 GBV_ILN_2336 GBV_ILN_2472 GBV_ILN_2522 GBV_ILN_2812 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4346 GBV_ILN_4367 GBV_ILN_4700 GBV_ILN_4753 35.16 ASE 42.14 ASE AR 6 2007 1 01 01 41-49 |
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Buttani, Valentina @@aut@@ Losi, Aba @@aut@@ Eggert, Thorsten @@aut@@ Krauss, Ulrich @@aut@@ Jaeger, Karl-Erich @@aut@@ Cao, Zhen @@aut@@ Gärtner, Wolfgang @@aut@@ |
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Buttani, Valentina |
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Buttani, Valentina ddc 620 bkl 35.16 bkl 42.14 Conformational analysis of the blue-light sensing protein YtvA reveals a competitive interface for LOV—LOV dimerization and interdomain interactions |
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620 ASE 35.16 bkl 42.14 bkl Conformational analysis of the blue-light sensing protein YtvA reveals a competitive interface for LOV—LOV dimerization and interdomain interactions |
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Conformational analysis of the blue-light sensing protein YtvA reveals a competitive interface for LOV—LOV dimerization and interdomain interactions |
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Conformational analysis of the blue-light sensing protein YtvA reveals a competitive interface for LOV—LOV dimerization and interdomain interactions |
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Buttani, Valentina |
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Photochemical & photobiological sciences |
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Buttani, Valentina Losi, Aba Eggert, Thorsten Krauss, Ulrich Jaeger, Karl-Erich Cao, Zhen Gärtner, Wolfgang |
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conformational analysis of the blue-light sensing protein ytva reveals a competitive interface for lov—lov dimerization and interdomain interactions |
| title_auth |
Conformational analysis of the blue-light sensing protein YtvA reveals a competitive interface for LOV—LOV dimerization and interdomain interactions |
| abstract |
Abstract The Bacillus subtilis protein YtvA is related to plant phototropins in that it senses UVA—blue-light by means of the flavin binding LOV domain, linked to a nucleotide-binding STAS domain. The structural basis for interdomain interactions and functional regulation are not known. Here we report the conformational analysis of three YtvA constructs, by means of size exclusion chromatography, circular dichroism (CD) and molecular docking simulations. The isolated YtvA-LOV domain (YLOV, aa 25–126) has a strong tendency to dimerize, prevented in full-length YtvA, but still observed in YLOV carrying the N-terminal extension (N-YLOV, aa 1–126). The analysis of CD data shows that both the N-terminal cap and the linker region (aa 127–147) between the LOV and the STAS domain are helical and that the central β-scaffold is distorted in the LOV domains dimers. The involvement of the central β-scaffold in dimerization is supported by docking simulation of the YLOV dimer and the importance of this region is highlighted by light-induced conformational changes, emerging from the CD data analysis. In YtvA, the β-strand fraction is notably less distorted and distinct light-driven changes in the loops/turn fraction are detected. The data uncover a common surface for LOV–LOV and intraprotein interaction, involving the central β-scaffold, and offer hints to investigate the molecular basis of light-activation and regulation in LOV proteins. © The Royal Society of Chemistry and Owner Societies 2007 |
| abstractGer |
Abstract The Bacillus subtilis protein YtvA is related to plant phototropins in that it senses UVA—blue-light by means of the flavin binding LOV domain, linked to a nucleotide-binding STAS domain. The structural basis for interdomain interactions and functional regulation are not known. Here we report the conformational analysis of three YtvA constructs, by means of size exclusion chromatography, circular dichroism (CD) and molecular docking simulations. The isolated YtvA-LOV domain (YLOV, aa 25–126) has a strong tendency to dimerize, prevented in full-length YtvA, but still observed in YLOV carrying the N-terminal extension (N-YLOV, aa 1–126). The analysis of CD data shows that both the N-terminal cap and the linker region (aa 127–147) between the LOV and the STAS domain are helical and that the central β-scaffold is distorted in the LOV domains dimers. The involvement of the central β-scaffold in dimerization is supported by docking simulation of the YLOV dimer and the importance of this region is highlighted by light-induced conformational changes, emerging from the CD data analysis. In YtvA, the β-strand fraction is notably less distorted and distinct light-driven changes in the loops/turn fraction are detected. The data uncover a common surface for LOV–LOV and intraprotein interaction, involving the central β-scaffold, and offer hints to investigate the molecular basis of light-activation and regulation in LOV proteins. © The Royal Society of Chemistry and Owner Societies 2007 |
| abstract_unstemmed |
Abstract The Bacillus subtilis protein YtvA is related to plant phototropins in that it senses UVA—blue-light by means of the flavin binding LOV domain, linked to a nucleotide-binding STAS domain. The structural basis for interdomain interactions and functional regulation are not known. Here we report the conformational analysis of three YtvA constructs, by means of size exclusion chromatography, circular dichroism (CD) and molecular docking simulations. The isolated YtvA-LOV domain (YLOV, aa 25–126) has a strong tendency to dimerize, prevented in full-length YtvA, but still observed in YLOV carrying the N-terminal extension (N-YLOV, aa 1–126). The analysis of CD data shows that both the N-terminal cap and the linker region (aa 127–147) between the LOV and the STAS domain are helical and that the central β-scaffold is distorted in the LOV domains dimers. The involvement of the central β-scaffold in dimerization is supported by docking simulation of the YLOV dimer and the importance of this region is highlighted by light-induced conformational changes, emerging from the CD data analysis. In YtvA, the β-strand fraction is notably less distorted and distinct light-driven changes in the loops/turn fraction are detected. The data uncover a common surface for LOV–LOV and intraprotein interaction, involving the central β-scaffold, and offer hints to investigate the molecular basis of light-activation and regulation in LOV proteins. © The Royal Society of Chemistry and Owner Societies 2007 |
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Conformational analysis of the blue-light sensing protein YtvA reveals a competitive interface for LOV—LOV dimerization and interdomain interactions |
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Losi, Aba Eggert, Thorsten Krauss, Ulrich Jaeger, Karl-Erich Cao, Zhen Gärtner, Wolfgang |
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10.1039/b610375h |
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2024-07-03T13:25:51.126Z |
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The structural basis for interdomain interactions and functional regulation are not known. Here we report the conformational analysis of three YtvA constructs, by means of size exclusion chromatography, circular dichroism (CD) and molecular docking simulations. The isolated YtvA-LOV domain (YLOV, aa 25–126) has a strong tendency to dimerize, prevented in full-length YtvA, but still observed in YLOV carrying the N-terminal extension (N-YLOV, aa 1–126). The analysis of CD data shows that both the N-terminal cap and the linker region (aa 127–147) between the LOV and the STAS domain are helical and that the central β-scaffold is distorted in the LOV domains dimers. The involvement of the central β-scaffold in dimerization is supported by docking simulation of the YLOV dimer and the importance of this region is highlighted by light-induced conformational changes, emerging from the CD data analysis. In YtvA, the β-strand fraction is notably less distorted and distinct light-driven changes in the loops/turn fraction are detected. 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