Structural Bases for the Regulation of CO Binding in the Archaeal Protoglobin from Methanosarcina acetivorans.

Studies of CO ligand binding revealed that two protein states with different ligand affinities exist in the protoglobin from Methanosarcina acetivorans (in MaPgb*, residue Cys(E20)101 was mutated to Ser). The switch between the two states occurs upon the ligation of MaPgb*. In this work, site-direct...
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Autor*in:	Lesley Tilleman [verfasserIn] Stefania Abbruzzetti [verfasserIn] Chiara Ciaccio [verfasserIn] Giampiero De Sanctis [verfasserIn] Marco Nardini [verfasserIn] Alessandra Pesce [verfasserIn] Filip Desmet [verfasserIn] Luc Moens [verfasserIn] Sabine Van Doorslaer [verfasserIn] Stefano Bruno [verfasserIn] Martino Bolognesi [verfasserIn] Paolo Ascenzi [verfasserIn] Massimo Coletta [verfasserIn] Cristiano Viappiani [verfasserIn] Sylvia Dewilde [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2015

Übergeordnetes Werk:	In: PLoS ONE - Public Library of Science (PLoS), 2007, 10(2015), 6, p e0125959
Übergeordnetes Werk:	volume:10 ; year:2015 ; number:6, p e0125959

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.1371/journal.pone.0125959

Katalog-ID:	DOAJ034623760

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520			\|a Studies of CO ligand binding revealed that two protein states with different ligand affinities exist in the protoglobin from Methanosarcina acetivorans (in MaPgb, residue Cys(E20)101 was mutated to Ser). The switch between the two states occurs upon the ligation of MaPgb. In this work, site-directed mutagenesis was used to explore the role of selected amino acids in ligand sensing and stabilization and in affecting the equilibrium between the "more reactive" and "less reactive" conformational states of MaPgb. A combination of experimental data obtained from electronic and resonance Raman absorption spectra, CO ligand-binding kinetics, and X-ray crystallography was employed. Three amino acids were assigned a critical role: Trp(60)B9, Tyr(61)B10, and Phe(93)E11. Trp(60)B9 and Tyr(61)B10 are involved in ligand stabilization in the distal heme pocket; the strength of their interaction was reflected by the spectra of the CO-ligated MaPgb and by the CO dissociation rate constants. In contrast, Phe(93)E11 is a key player in sensing the heme-bound ligand and promotes the rotation of the Trp(60)B9 side chain, thus favoring ligand stabilization. Although the structural bases of the fast CO binding rate constant of MaPgb* are still unclear, Trp(60)B9, Tyr(61)B10, and Phe(93)E11 play a role in regulating heme/ligand affinity.
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912			\|a GBV_ILN_4325
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allfields	10.1371/journal.pone.0125959 doi (DE-627)DOAJ034623760 (DE-599)DOAJ226faa0db1ac4c2fbaa3c95f40ade699 DE-627 ger DE-627 rakwb eng Lesley Tilleman verfasserin aut Structural Bases for the Regulation of CO Binding in the Archaeal Protoglobin from Methanosarcina acetivorans. 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Studies of CO ligand binding revealed that two protein states with different ligand affinities exist in the protoglobin from Methanosarcina acetivorans (in MaPgb, residue Cys(E20)101 was mutated to Ser). The switch between the two states occurs upon the ligation of MaPgb. In this work, site-directed mutagenesis was used to explore the role of selected amino acids in ligand sensing and stabilization and in affecting the equilibrium between the "more reactive" and "less reactive" conformational states of MaPgb. A combination of experimental data obtained from electronic and resonance Raman absorption spectra, CO ligand-binding kinetics, and X-ray crystallography was employed. Three amino acids were assigned a critical role: Trp(60)B9, Tyr(61)B10, and Phe(93)E11. Trp(60)B9 and Tyr(61)B10 are involved in ligand stabilization in the distal heme pocket; the strength of their interaction was reflected by the spectra of the CO-ligated MaPgb and by the CO dissociation rate constants. In contrast, Phe(93)E11 is a key player in sensing the heme-bound ligand and promotes the rotation of the Trp(60)B9 side chain, thus favoring ligand stabilization. Although the structural bases of the fast CO binding rate constant of MaPgb* are still unclear, Trp(60)B9, Tyr(61)B10, and Phe(93)E11 play a role in regulating heme/ligand affinity. Medicine R Science Q Stefania Abbruzzetti verfasserin aut Chiara Ciaccio verfasserin aut Giampiero De Sanctis verfasserin aut Marco Nardini verfasserin aut Alessandra Pesce verfasserin aut Filip Desmet verfasserin aut Luc Moens verfasserin aut Sabine Van Doorslaer verfasserin aut Stefano Bruno verfasserin aut Martino Bolognesi verfasserin aut Paolo Ascenzi verfasserin aut Massimo Coletta verfasserin aut Cristiano Viappiani verfasserin aut Sylvia Dewilde verfasserin aut In PLoS ONE Public Library of Science (PLoS), 2007 10(2015), 6, p e0125959 (DE-627)523574592 (DE-600)2267670-3 19326203 nnns volume:10 year:2015 number:6, p e0125959 https://doi.org/10.1371/journal.pone.0125959 kostenfrei https://doaj.org/article/226faa0db1ac4c2fbaa3c95f40ade699 kostenfrei http://europepmc.org/articles/PMC4457829?pdf=render kostenfrei https://doaj.org/toc/1932-6203 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_34 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_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_235 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_2522 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 10 2015 6, p e0125959
spelling	10.1371/journal.pone.0125959 doi (DE-627)DOAJ034623760 (DE-599)DOAJ226faa0db1ac4c2fbaa3c95f40ade699 DE-627 ger DE-627 rakwb eng Lesley Tilleman verfasserin aut Structural Bases for the Regulation of CO Binding in the Archaeal Protoglobin from Methanosarcina acetivorans. 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Studies of CO ligand binding revealed that two protein states with different ligand affinities exist in the protoglobin from Methanosarcina acetivorans (in MaPgb, residue Cys(E20)101 was mutated to Ser). The switch between the two states occurs upon the ligation of MaPgb. In this work, site-directed mutagenesis was used to explore the role of selected amino acids in ligand sensing and stabilization and in affecting the equilibrium between the "more reactive" and "less reactive" conformational states of MaPgb. A combination of experimental data obtained from electronic and resonance Raman absorption spectra, CO ligand-binding kinetics, and X-ray crystallography was employed. Three amino acids were assigned a critical role: Trp(60)B9, Tyr(61)B10, and Phe(93)E11. Trp(60)B9 and Tyr(61)B10 are involved in ligand stabilization in the distal heme pocket; the strength of their interaction was reflected by the spectra of the CO-ligated MaPgb and by the CO dissociation rate constants. In contrast, Phe(93)E11 is a key player in sensing the heme-bound ligand and promotes the rotation of the Trp(60)B9 side chain, thus favoring ligand stabilization. Although the structural bases of the fast CO binding rate constant of MaPgb* are still unclear, Trp(60)B9, Tyr(61)B10, and Phe(93)E11 play a role in regulating heme/ligand affinity. Medicine R Science Q Stefania Abbruzzetti verfasserin aut Chiara Ciaccio verfasserin aut Giampiero De Sanctis verfasserin aut Marco Nardini verfasserin aut Alessandra Pesce verfasserin aut Filip Desmet verfasserin aut Luc Moens verfasserin aut Sabine Van Doorslaer verfasserin aut Stefano Bruno verfasserin aut Martino Bolognesi verfasserin aut Paolo Ascenzi verfasserin aut Massimo Coletta verfasserin aut Cristiano Viappiani verfasserin aut Sylvia Dewilde verfasserin aut In PLoS ONE Public Library of Science (PLoS), 2007 10(2015), 6, p e0125959 (DE-627)523574592 (DE-600)2267670-3 19326203 nnns volume:10 year:2015 number:6, p e0125959 https://doi.org/10.1371/journal.pone.0125959 kostenfrei https://doaj.org/article/226faa0db1ac4c2fbaa3c95f40ade699 kostenfrei http://europepmc.org/articles/PMC4457829?pdf=render kostenfrei https://doaj.org/toc/1932-6203 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_34 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_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_235 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_2522 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 10 2015 6, p e0125959
allfields_unstemmed	10.1371/journal.pone.0125959 doi (DE-627)DOAJ034623760 (DE-599)DOAJ226faa0db1ac4c2fbaa3c95f40ade699 DE-627 ger DE-627 rakwb eng Lesley Tilleman verfasserin aut Structural Bases for the Regulation of CO Binding in the Archaeal Protoglobin from Methanosarcina acetivorans. 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Studies of CO ligand binding revealed that two protein states with different ligand affinities exist in the protoglobin from Methanosarcina acetivorans (in MaPgb, residue Cys(E20)101 was mutated to Ser). The switch between the two states occurs upon the ligation of MaPgb. In this work, site-directed mutagenesis was used to explore the role of selected amino acids in ligand sensing and stabilization and in affecting the equilibrium between the "more reactive" and "less reactive" conformational states of MaPgb. A combination of experimental data obtained from electronic and resonance Raman absorption spectra, CO ligand-binding kinetics, and X-ray crystallography was employed. Three amino acids were assigned a critical role: Trp(60)B9, Tyr(61)B10, and Phe(93)E11. Trp(60)B9 and Tyr(61)B10 are involved in ligand stabilization in the distal heme pocket; the strength of their interaction was reflected by the spectra of the CO-ligated MaPgb and by the CO dissociation rate constants. In contrast, Phe(93)E11 is a key player in sensing the heme-bound ligand and promotes the rotation of the Trp(60)B9 side chain, thus favoring ligand stabilization. Although the structural bases of the fast CO binding rate constant of MaPgb* are still unclear, Trp(60)B9, Tyr(61)B10, and Phe(93)E11 play a role in regulating heme/ligand affinity. Medicine R Science Q Stefania Abbruzzetti verfasserin aut Chiara Ciaccio verfasserin aut Giampiero De Sanctis verfasserin aut Marco Nardini verfasserin aut Alessandra Pesce verfasserin aut Filip Desmet verfasserin aut Luc Moens verfasserin aut Sabine Van Doorslaer verfasserin aut Stefano Bruno verfasserin aut Martino Bolognesi verfasserin aut Paolo Ascenzi verfasserin aut Massimo Coletta verfasserin aut Cristiano Viappiani verfasserin aut Sylvia Dewilde verfasserin aut In PLoS ONE Public Library of Science (PLoS), 2007 10(2015), 6, p e0125959 (DE-627)523574592 (DE-600)2267670-3 19326203 nnns volume:10 year:2015 number:6, p e0125959 https://doi.org/10.1371/journal.pone.0125959 kostenfrei https://doaj.org/article/226faa0db1ac4c2fbaa3c95f40ade699 kostenfrei http://europepmc.org/articles/PMC4457829?pdf=render kostenfrei https://doaj.org/toc/1932-6203 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_34 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_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_235 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_2522 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 10 2015 6, p e0125959
allfieldsGer	10.1371/journal.pone.0125959 doi (DE-627)DOAJ034623760 (DE-599)DOAJ226faa0db1ac4c2fbaa3c95f40ade699 DE-627 ger DE-627 rakwb eng Lesley Tilleman verfasserin aut Structural Bases for the Regulation of CO Binding in the Archaeal Protoglobin from Methanosarcina acetivorans. 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Studies of CO ligand binding revealed that two protein states with different ligand affinities exist in the protoglobin from Methanosarcina acetivorans (in MaPgb, residue Cys(E20)101 was mutated to Ser). The switch between the two states occurs upon the ligation of MaPgb. In this work, site-directed mutagenesis was used to explore the role of selected amino acids in ligand sensing and stabilization and in affecting the equilibrium between the "more reactive" and "less reactive" conformational states of MaPgb. A combination of experimental data obtained from electronic and resonance Raman absorption spectra, CO ligand-binding kinetics, and X-ray crystallography was employed. Three amino acids were assigned a critical role: Trp(60)B9, Tyr(61)B10, and Phe(93)E11. Trp(60)B9 and Tyr(61)B10 are involved in ligand stabilization in the distal heme pocket; the strength of their interaction was reflected by the spectra of the CO-ligated MaPgb and by the CO dissociation rate constants. In contrast, Phe(93)E11 is a key player in sensing the heme-bound ligand and promotes the rotation of the Trp(60)B9 side chain, thus favoring ligand stabilization. Although the structural bases of the fast CO binding rate constant of MaPgb* are still unclear, Trp(60)B9, Tyr(61)B10, and Phe(93)E11 play a role in regulating heme/ligand affinity. Medicine R Science Q Stefania Abbruzzetti verfasserin aut Chiara Ciaccio verfasserin aut Giampiero De Sanctis verfasserin aut Marco Nardini verfasserin aut Alessandra Pesce verfasserin aut Filip Desmet verfasserin aut Luc Moens verfasserin aut Sabine Van Doorslaer verfasserin aut Stefano Bruno verfasserin aut Martino Bolognesi verfasserin aut Paolo Ascenzi verfasserin aut Massimo Coletta verfasserin aut Cristiano Viappiani verfasserin aut Sylvia Dewilde verfasserin aut In PLoS ONE Public Library of Science (PLoS), 2007 10(2015), 6, p e0125959 (DE-627)523574592 (DE-600)2267670-3 19326203 nnns volume:10 year:2015 number:6, p e0125959 https://doi.org/10.1371/journal.pone.0125959 kostenfrei https://doaj.org/article/226faa0db1ac4c2fbaa3c95f40ade699 kostenfrei http://europepmc.org/articles/PMC4457829?pdf=render kostenfrei https://doaj.org/toc/1932-6203 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_34 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_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_235 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_2522 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 10 2015 6, p e0125959
allfieldsSound	10.1371/journal.pone.0125959 doi (DE-627)DOAJ034623760 (DE-599)DOAJ226faa0db1ac4c2fbaa3c95f40ade699 DE-627 ger DE-627 rakwb eng Lesley Tilleman verfasserin aut Structural Bases for the Regulation of CO Binding in the Archaeal Protoglobin from Methanosarcina acetivorans. 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Studies of CO ligand binding revealed that two protein states with different ligand affinities exist in the protoglobin from Methanosarcina acetivorans (in MaPgb, residue Cys(E20)101 was mutated to Ser). The switch between the two states occurs upon the ligation of MaPgb. In this work, site-directed mutagenesis was used to explore the role of selected amino acids in ligand sensing and stabilization and in affecting the equilibrium between the "more reactive" and "less reactive" conformational states of MaPgb. A combination of experimental data obtained from electronic and resonance Raman absorption spectra, CO ligand-binding kinetics, and X-ray crystallography was employed. Three amino acids were assigned a critical role: Trp(60)B9, Tyr(61)B10, and Phe(93)E11. Trp(60)B9 and Tyr(61)B10 are involved in ligand stabilization in the distal heme pocket; the strength of their interaction was reflected by the spectra of the CO-ligated MaPgb and by the CO dissociation rate constants. In contrast, Phe(93)E11 is a key player in sensing the heme-bound ligand and promotes the rotation of the Trp(60)B9 side chain, thus favoring ligand stabilization. Although the structural bases of the fast CO binding rate constant of MaPgb* are still unclear, Trp(60)B9, Tyr(61)B10, and Phe(93)E11 play a role in regulating heme/ligand affinity. Medicine R Science Q Stefania Abbruzzetti verfasserin aut Chiara Ciaccio verfasserin aut Giampiero De Sanctis verfasserin aut Marco Nardini verfasserin aut Alessandra Pesce verfasserin aut Filip Desmet verfasserin aut Luc Moens verfasserin aut Sabine Van Doorslaer verfasserin aut Stefano Bruno verfasserin aut Martino Bolognesi verfasserin aut Paolo Ascenzi verfasserin aut Massimo Coletta verfasserin aut Cristiano Viappiani verfasserin aut Sylvia Dewilde verfasserin aut In PLoS ONE Public Library of Science (PLoS), 2007 10(2015), 6, p e0125959 (DE-627)523574592 (DE-600)2267670-3 19326203 nnns volume:10 year:2015 number:6, p e0125959 https://doi.org/10.1371/journal.pone.0125959 kostenfrei https://doaj.org/article/226faa0db1ac4c2fbaa3c95f40ade699 kostenfrei http://europepmc.org/articles/PMC4457829?pdf=render kostenfrei https://doaj.org/toc/1932-6203 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_34 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_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_235 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2190 GBV_ILN_2522 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 10 2015 6, p e0125959
language	English
source	In PLoS ONE 10(2015), 6, p e0125959 volume:10 year:2015 number:6, p e0125959
sourceStr	In PLoS ONE 10(2015), 6, p e0125959 volume:10 year:2015 number:6, p e0125959
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Medicine R Science Q
isfreeaccess_bool	true
container_title	PLoS ONE
authorswithroles_txt_mv	Lesley Tilleman @@aut@@ Stefania Abbruzzetti @@aut@@ Chiara Ciaccio @@aut@@ Giampiero De Sanctis @@aut@@ Marco Nardini @@aut@@ Alessandra Pesce @@aut@@ Filip Desmet @@aut@@ Luc Moens @@aut@@ Sabine Van Doorslaer @@aut@@ Stefano Bruno @@aut@@ Martino Bolognesi @@aut@@ Paolo Ascenzi @@aut@@ Massimo Coletta @@aut@@ Cristiano Viappiani @@aut@@ Sylvia Dewilde @@aut@@
publishDateDaySort_date	2015-01-01T00:00:00Z
hierarchy_top_id	523574592
id	DOAJ034623760
language_de	englisch
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author	Lesley Tilleman
spellingShingle	Lesley Tilleman misc Medicine misc R misc Science misc Q Structural Bases for the Regulation of CO Binding in the Archaeal Protoglobin from Methanosarcina acetivorans.
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topic_title	Structural Bases for the Regulation of CO Binding in the Archaeal Protoglobin from Methanosarcina acetivorans
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title	Structural Bases for the Regulation of CO Binding in the Archaeal Protoglobin from Methanosarcina acetivorans.
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title_full	Structural Bases for the Regulation of CO Binding in the Archaeal Protoglobin from Methanosarcina acetivorans
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title_sort	structural bases for the regulation of co binding in the archaeal protoglobin from methanosarcina acetivorans
title_auth	Structural Bases for the Regulation of CO Binding in the Archaeal Protoglobin from Methanosarcina acetivorans.
abstract	Studies of CO ligand binding revealed that two protein states with different ligand affinities exist in the protoglobin from Methanosarcina acetivorans (in MaPgb, residue Cys(E20)101 was mutated to Ser). The switch between the two states occurs upon the ligation of MaPgb. In this work, site-directed mutagenesis was used to explore the role of selected amino acids in ligand sensing and stabilization and in affecting the equilibrium between the "more reactive" and "less reactive" conformational states of MaPgb. A combination of experimental data obtained from electronic and resonance Raman absorption spectra, CO ligand-binding kinetics, and X-ray crystallography was employed. Three amino acids were assigned a critical role: Trp(60)B9, Tyr(61)B10, and Phe(93)E11. Trp(60)B9 and Tyr(61)B10 are involved in ligand stabilization in the distal heme pocket; the strength of their interaction was reflected by the spectra of the CO-ligated MaPgb and by the CO dissociation rate constants. In contrast, Phe(93)E11 is a key player in sensing the heme-bound ligand and promotes the rotation of the Trp(60)B9 side chain, thus favoring ligand stabilization. Although the structural bases of the fast CO binding rate constant of MaPgb* are still unclear, Trp(60)B9, Tyr(61)B10, and Phe(93)E11 play a role in regulating heme/ligand affinity.
abstractGer	Studies of CO ligand binding revealed that two protein states with different ligand affinities exist in the protoglobin from Methanosarcina acetivorans (in MaPgb, residue Cys(E20)101 was mutated to Ser). The switch between the two states occurs upon the ligation of MaPgb. In this work, site-directed mutagenesis was used to explore the role of selected amino acids in ligand sensing and stabilization and in affecting the equilibrium between the "more reactive" and "less reactive" conformational states of MaPgb. A combination of experimental data obtained from electronic and resonance Raman absorption spectra, CO ligand-binding kinetics, and X-ray crystallography was employed. Three amino acids were assigned a critical role: Trp(60)B9, Tyr(61)B10, and Phe(93)E11. Trp(60)B9 and Tyr(61)B10 are involved in ligand stabilization in the distal heme pocket; the strength of their interaction was reflected by the spectra of the CO-ligated MaPgb and by the CO dissociation rate constants. In contrast, Phe(93)E11 is a key player in sensing the heme-bound ligand and promotes the rotation of the Trp(60)B9 side chain, thus favoring ligand stabilization. Although the structural bases of the fast CO binding rate constant of MaPgb* are still unclear, Trp(60)B9, Tyr(61)B10, and Phe(93)E11 play a role in regulating heme/ligand affinity.
abstract_unstemmed	Studies of CO ligand binding revealed that two protein states with different ligand affinities exist in the protoglobin from Methanosarcina acetivorans (in MaPgb, residue Cys(E20)101 was mutated to Ser). The switch between the two states occurs upon the ligation of MaPgb. In this work, site-directed mutagenesis was used to explore the role of selected amino acids in ligand sensing and stabilization and in affecting the equilibrium between the "more reactive" and "less reactive" conformational states of MaPgb. A combination of experimental data obtained from electronic and resonance Raman absorption spectra, CO ligand-binding kinetics, and X-ray crystallography was employed. Three amino acids were assigned a critical role: Trp(60)B9, Tyr(61)B10, and Phe(93)E11. Trp(60)B9 and Tyr(61)B10 are involved in ligand stabilization in the distal heme pocket; the strength of their interaction was reflected by the spectra of the CO-ligated MaPgb and by the CO dissociation rate constants. In contrast, Phe(93)E11 is a key player in sensing the heme-bound ligand and promotes the rotation of the Trp(60)B9 side chain, thus favoring ligand stabilization. Although the structural bases of the fast CO binding rate constant of MaPgb* are still unclear, Trp(60)B9, Tyr(61)B10, and Phe(93)E11 play a role in regulating heme/ligand affinity.
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title_short	Structural Bases for the Regulation of CO Binding in the Archaeal Protoglobin from Methanosarcina acetivorans.
url	https://doi.org/10.1371/journal.pone.0125959 https://doaj.org/article/226faa0db1ac4c2fbaa3c95f40ade699 http://europepmc.org/articles/PMC4457829?pdf=render https://doaj.org/toc/1932-6203
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Structural Bases for the Regulation of CO Binding in the Archaeal Protoglobin from Methanosarcina acetivorans.

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