Structural Analysis of the Partially Disordered Protein EspK from <i<Mycobacterium Tuberculosis</i<
For centuries, tuberculosis has been a worldwide burden for human health, and gaps in our understanding of its pathogenesis have hampered the development of new treatments. ESX-1 is a complex machinery responsible for the secretion of virulence factors that manipulate the host response. Despite the...
Ausführliche Beschreibung
Autor*in: |
Abril Gijsbers [verfasserIn] Nuria Sánchez-Puig [verfasserIn] Ye Gao [verfasserIn] Peter J. Peters [verfasserIn] Raimond B. G. Ravelli [verfasserIn] Dritan Siliqi [verfasserIn] |
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E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2020 |
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Übergeordnetes Werk: |
In: Crystals - MDPI AG, 2011, 11(2020), 1, p 18 |
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Übergeordnetes Werk: |
volume:11 ; year:2020 ; number:1, p 18 |
Links: |
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DOI / URN: |
10.3390/cryst11010018 |
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Katalog-ID: |
DOAJ087108712 |
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10.3390/cryst11010018 doi (DE-627)DOAJ087108712 (DE-599)DOAJ8d83196956f14cc28472aff1fc639e3b DE-627 ger DE-627 rakwb eng QD901-999 Abril Gijsbers verfasserin aut Structural Analysis of the Partially Disordered Protein EspK from <i<Mycobacterium Tuberculosis</i< 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier For centuries, tuberculosis has been a worldwide burden for human health, and gaps in our understanding of its pathogenesis have hampered the development of new treatments. ESX-1 is a complex machinery responsible for the secretion of virulence factors that manipulate the host response. Despite the importance of these secreted proteins for pathogenicity, only a few of them have been structurally and functionally characterised. Here, we describe a structural study of the ESX-secretion associated protein K (EspK), a 74 kDa protein known to be essential for the secretion of other substrates and the cytolytic effects of ESX-1. Small-Angle X-ray Scattering (SAXS) data show that EspK is a long molecule with a maximal dimension of 228 Å. It consists of two independent folded regions at each end of the protein connected by a flexible unstructured region driving the protein to coexist as an ensemble of conformations. Limited proteolysis identified a 26 kDa globular domain at the C-terminus of the protein consisting of a mixture of α-helices and β-strands, as shown by circular dichroism (CD) and SAXS. In contrast, the N-terminal portion is mainly helical with an elongated shape. Sequence conservation suggests that this architecture is preserved amongst the different mycobacteria species, proposing specific roles for the N- and C-terminal domains assisted by the middle flexible linker. disordered region EspK ESX-1 SAXS Crystallography Nuria Sánchez-Puig verfasserin aut Ye Gao verfasserin aut Peter J. Peters verfasserin aut Raimond B. G. Ravelli verfasserin aut Dritan Siliqi verfasserin aut In Crystals MDPI AG, 2011 11(2020), 1, p 18 (DE-627)718303067 (DE-600)2661516-2 20734352 nnns volume:11 year:2020 number:1, p 18 https://doi.org/10.3390/cryst11010018 kostenfrei https://doaj.org/article/8d83196956f14cc28472aff1fc639e3b kostenfrei https://www.mdpi.com/2073-4352/11/1/18 kostenfrei https://doaj.org/toc/2073-4352 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 11 2020 1, p 18 |
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10.3390/cryst11010018 doi (DE-627)DOAJ087108712 (DE-599)DOAJ8d83196956f14cc28472aff1fc639e3b DE-627 ger DE-627 rakwb eng QD901-999 Abril Gijsbers verfasserin aut Structural Analysis of the Partially Disordered Protein EspK from <i<Mycobacterium Tuberculosis</i< 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier For centuries, tuberculosis has been a worldwide burden for human health, and gaps in our understanding of its pathogenesis have hampered the development of new treatments. ESX-1 is a complex machinery responsible for the secretion of virulence factors that manipulate the host response. Despite the importance of these secreted proteins for pathogenicity, only a few of them have been structurally and functionally characterised. Here, we describe a structural study of the ESX-secretion associated protein K (EspK), a 74 kDa protein known to be essential for the secretion of other substrates and the cytolytic effects of ESX-1. Small-Angle X-ray Scattering (SAXS) data show that EspK is a long molecule with a maximal dimension of 228 Å. It consists of two independent folded regions at each end of the protein connected by a flexible unstructured region driving the protein to coexist as an ensemble of conformations. Limited proteolysis identified a 26 kDa globular domain at the C-terminus of the protein consisting of a mixture of α-helices and β-strands, as shown by circular dichroism (CD) and SAXS. In contrast, the N-terminal portion is mainly helical with an elongated shape. Sequence conservation suggests that this architecture is preserved amongst the different mycobacteria species, proposing specific roles for the N- and C-terminal domains assisted by the middle flexible linker. disordered region EspK ESX-1 SAXS Crystallography Nuria Sánchez-Puig verfasserin aut Ye Gao verfasserin aut Peter J. Peters verfasserin aut Raimond B. G. Ravelli verfasserin aut Dritan Siliqi verfasserin aut In Crystals MDPI AG, 2011 11(2020), 1, p 18 (DE-627)718303067 (DE-600)2661516-2 20734352 nnns volume:11 year:2020 number:1, p 18 https://doi.org/10.3390/cryst11010018 kostenfrei https://doaj.org/article/8d83196956f14cc28472aff1fc639e3b kostenfrei https://www.mdpi.com/2073-4352/11/1/18 kostenfrei https://doaj.org/toc/2073-4352 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 11 2020 1, p 18 |
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10.3390/cryst11010018 doi (DE-627)DOAJ087108712 (DE-599)DOAJ8d83196956f14cc28472aff1fc639e3b DE-627 ger DE-627 rakwb eng QD901-999 Abril Gijsbers verfasserin aut Structural Analysis of the Partially Disordered Protein EspK from <i<Mycobacterium Tuberculosis</i< 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier For centuries, tuberculosis has been a worldwide burden for human health, and gaps in our understanding of its pathogenesis have hampered the development of new treatments. ESX-1 is a complex machinery responsible for the secretion of virulence factors that manipulate the host response. Despite the importance of these secreted proteins for pathogenicity, only a few of them have been structurally and functionally characterised. Here, we describe a structural study of the ESX-secretion associated protein K (EspK), a 74 kDa protein known to be essential for the secretion of other substrates and the cytolytic effects of ESX-1. Small-Angle X-ray Scattering (SAXS) data show that EspK is a long molecule with a maximal dimension of 228 Å. It consists of two independent folded regions at each end of the protein connected by a flexible unstructured region driving the protein to coexist as an ensemble of conformations. Limited proteolysis identified a 26 kDa globular domain at the C-terminus of the protein consisting of a mixture of α-helices and β-strands, as shown by circular dichroism (CD) and SAXS. In contrast, the N-terminal portion is mainly helical with an elongated shape. Sequence conservation suggests that this architecture is preserved amongst the different mycobacteria species, proposing specific roles for the N- and C-terminal domains assisted by the middle flexible linker. disordered region EspK ESX-1 SAXS Crystallography Nuria Sánchez-Puig verfasserin aut Ye Gao verfasserin aut Peter J. Peters verfasserin aut Raimond B. G. Ravelli verfasserin aut Dritan Siliqi verfasserin aut In Crystals MDPI AG, 2011 11(2020), 1, p 18 (DE-627)718303067 (DE-600)2661516-2 20734352 nnns volume:11 year:2020 number:1, p 18 https://doi.org/10.3390/cryst11010018 kostenfrei https://doaj.org/article/8d83196956f14cc28472aff1fc639e3b kostenfrei https://www.mdpi.com/2073-4352/11/1/18 kostenfrei https://doaj.org/toc/2073-4352 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 11 2020 1, p 18 |
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10.3390/cryst11010018 doi (DE-627)DOAJ087108712 (DE-599)DOAJ8d83196956f14cc28472aff1fc639e3b DE-627 ger DE-627 rakwb eng QD901-999 Abril Gijsbers verfasserin aut Structural Analysis of the Partially Disordered Protein EspK from <i<Mycobacterium Tuberculosis</i< 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier For centuries, tuberculosis has been a worldwide burden for human health, and gaps in our understanding of its pathogenesis have hampered the development of new treatments. ESX-1 is a complex machinery responsible for the secretion of virulence factors that manipulate the host response. Despite the importance of these secreted proteins for pathogenicity, only a few of them have been structurally and functionally characterised. Here, we describe a structural study of the ESX-secretion associated protein K (EspK), a 74 kDa protein known to be essential for the secretion of other substrates and the cytolytic effects of ESX-1. Small-Angle X-ray Scattering (SAXS) data show that EspK is a long molecule with a maximal dimension of 228 Å. It consists of two independent folded regions at each end of the protein connected by a flexible unstructured region driving the protein to coexist as an ensemble of conformations. Limited proteolysis identified a 26 kDa globular domain at the C-terminus of the protein consisting of a mixture of α-helices and β-strands, as shown by circular dichroism (CD) and SAXS. In contrast, the N-terminal portion is mainly helical with an elongated shape. Sequence conservation suggests that this architecture is preserved amongst the different mycobacteria species, proposing specific roles for the N- and C-terminal domains assisted by the middle flexible linker. disordered region EspK ESX-1 SAXS Crystallography Nuria Sánchez-Puig verfasserin aut Ye Gao verfasserin aut Peter J. Peters verfasserin aut Raimond B. G. Ravelli verfasserin aut Dritan Siliqi verfasserin aut In Crystals MDPI AG, 2011 11(2020), 1, p 18 (DE-627)718303067 (DE-600)2661516-2 20734352 nnns volume:11 year:2020 number:1, p 18 https://doi.org/10.3390/cryst11010018 kostenfrei https://doaj.org/article/8d83196956f14cc28472aff1fc639e3b kostenfrei https://www.mdpi.com/2073-4352/11/1/18 kostenfrei https://doaj.org/toc/2073-4352 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 11 2020 1, p 18 |
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10.3390/cryst11010018 doi (DE-627)DOAJ087108712 (DE-599)DOAJ8d83196956f14cc28472aff1fc639e3b DE-627 ger DE-627 rakwb eng QD901-999 Abril Gijsbers verfasserin aut Structural Analysis of the Partially Disordered Protein EspK from <i<Mycobacterium Tuberculosis</i< 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier For centuries, tuberculosis has been a worldwide burden for human health, and gaps in our understanding of its pathogenesis have hampered the development of new treatments. ESX-1 is a complex machinery responsible for the secretion of virulence factors that manipulate the host response. Despite the importance of these secreted proteins for pathogenicity, only a few of them have been structurally and functionally characterised. Here, we describe a structural study of the ESX-secretion associated protein K (EspK), a 74 kDa protein known to be essential for the secretion of other substrates and the cytolytic effects of ESX-1. Small-Angle X-ray Scattering (SAXS) data show that EspK is a long molecule with a maximal dimension of 228 Å. It consists of two independent folded regions at each end of the protein connected by a flexible unstructured region driving the protein to coexist as an ensemble of conformations. Limited proteolysis identified a 26 kDa globular domain at the C-terminus of the protein consisting of a mixture of α-helices and β-strands, as shown by circular dichroism (CD) and SAXS. In contrast, the N-terminal portion is mainly helical with an elongated shape. Sequence conservation suggests that this architecture is preserved amongst the different mycobacteria species, proposing specific roles for the N- and C-terminal domains assisted by the middle flexible linker. disordered region EspK ESX-1 SAXS Crystallography Nuria Sánchez-Puig verfasserin aut Ye Gao verfasserin aut Peter J. Peters verfasserin aut Raimond B. G. Ravelli verfasserin aut Dritan Siliqi verfasserin aut In Crystals MDPI AG, 2011 11(2020), 1, p 18 (DE-627)718303067 (DE-600)2661516-2 20734352 nnns volume:11 year:2020 number:1, p 18 https://doi.org/10.3390/cryst11010018 kostenfrei https://doaj.org/article/8d83196956f14cc28472aff1fc639e3b kostenfrei https://www.mdpi.com/2073-4352/11/1/18 kostenfrei https://doaj.org/toc/2073-4352 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4335 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 11 2020 1, p 18 |
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Structural Analysis of the Partially Disordered Protein EspK from <i<Mycobacterium Tuberculosis</i< |
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For centuries, tuberculosis has been a worldwide burden for human health, and gaps in our understanding of its pathogenesis have hampered the development of new treatments. ESX-1 is a complex machinery responsible for the secretion of virulence factors that manipulate the host response. Despite the importance of these secreted proteins for pathogenicity, only a few of them have been structurally and functionally characterised. Here, we describe a structural study of the ESX-secretion associated protein K (EspK), a 74 kDa protein known to be essential for the secretion of other substrates and the cytolytic effects of ESX-1. Small-Angle X-ray Scattering (SAXS) data show that EspK is a long molecule with a maximal dimension of 228 Å. It consists of two independent folded regions at each end of the protein connected by a flexible unstructured region driving the protein to coexist as an ensemble of conformations. Limited proteolysis identified a 26 kDa globular domain at the C-terminus of the protein consisting of a mixture of α-helices and β-strands, as shown by circular dichroism (CD) and SAXS. In contrast, the N-terminal portion is mainly helical with an elongated shape. Sequence conservation suggests that this architecture is preserved amongst the different mycobacteria species, proposing specific roles for the N- and C-terminal domains assisted by the middle flexible linker. |
abstractGer |
For centuries, tuberculosis has been a worldwide burden for human health, and gaps in our understanding of its pathogenesis have hampered the development of new treatments. ESX-1 is a complex machinery responsible for the secretion of virulence factors that manipulate the host response. Despite the importance of these secreted proteins for pathogenicity, only a few of them have been structurally and functionally characterised. Here, we describe a structural study of the ESX-secretion associated protein K (EspK), a 74 kDa protein known to be essential for the secretion of other substrates and the cytolytic effects of ESX-1. Small-Angle X-ray Scattering (SAXS) data show that EspK is a long molecule with a maximal dimension of 228 Å. It consists of two independent folded regions at each end of the protein connected by a flexible unstructured region driving the protein to coexist as an ensemble of conformations. Limited proteolysis identified a 26 kDa globular domain at the C-terminus of the protein consisting of a mixture of α-helices and β-strands, as shown by circular dichroism (CD) and SAXS. In contrast, the N-terminal portion is mainly helical with an elongated shape. Sequence conservation suggests that this architecture is preserved amongst the different mycobacteria species, proposing specific roles for the N- and C-terminal domains assisted by the middle flexible linker. |
abstract_unstemmed |
For centuries, tuberculosis has been a worldwide burden for human health, and gaps in our understanding of its pathogenesis have hampered the development of new treatments. ESX-1 is a complex machinery responsible for the secretion of virulence factors that manipulate the host response. Despite the importance of these secreted proteins for pathogenicity, only a few of them have been structurally and functionally characterised. Here, we describe a structural study of the ESX-secretion associated protein K (EspK), a 74 kDa protein known to be essential for the secretion of other substrates and the cytolytic effects of ESX-1. Small-Angle X-ray Scattering (SAXS) data show that EspK is a long molecule with a maximal dimension of 228 Å. It consists of two independent folded regions at each end of the protein connected by a flexible unstructured region driving the protein to coexist as an ensemble of conformations. Limited proteolysis identified a 26 kDa globular domain at the C-terminus of the protein consisting of a mixture of α-helices and β-strands, as shown by circular dichroism (CD) and SAXS. In contrast, the N-terminal portion is mainly helical with an elongated shape. Sequence conservation suggests that this architecture is preserved amongst the different mycobacteria species, proposing specific roles for the N- and C-terminal domains assisted by the middle flexible linker. |
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Structural Analysis of the Partially Disordered Protein EspK from <i<Mycobacterium Tuberculosis</i< |
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7.3999987 |