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Structure of cytochrome c7 from Desulfuromonas acetoxidans at 1.9 Å resolution.

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Title: Structure of cytochrome c7 from Desulfuromonas acetoxidans at 1.9 Å resolution.
Authors: Czjzek, Mirjam1 czjzek@afmb.cnrs-mrs.fr, Arnoux, Pascal1, Haser, Richard2, Shepardc, William3
Source: Acta Crystallographica: Section D (Wiley-Blackwell). May2001, Vol. 57 Issue 5, p670-678. 9p.
Subjects: Cytochromes, Bacteria, Proteins, Metals, Biotechnology, Porphyrins
Abstract: Multihaem cytochromes play a key role in electron-transport reactions in the periplasm of sulfate- and sulfur-reducing bacteria. The redox proteins grouped in the c3 superfamily also display metal-reducing activities, which make them interesting biotechnological tools. The crystal structure of the fully oxidized cytochrome c7 from Desulfuromonas acetoxidans has been solved by combined molecular- replacement and MAD methods. The structure has been refined at 1.9 Å resolution to an R value of 19.1% (Rfree = 24.3%) and includes three haems and 116 water molecules. The protein displays the cytochrome c3 fold in a highly minimized form, while haem 2 and the surrounding protein environment are missing. The geometry of haem packing and of the haem axial ligands and propionates are described and compared with that of c3 cytochromes. The crystal structure is compared with the solution structure recently obtained by NMR methods and with its homologue cytochromes of the c3 superfamily. Comparison of the high number of available structures makes it possible to analyze the structural role of the few highly conserved residues, in addition to the cysteines and histidines that link the porphyrin rings and the Fe atoms to the protein chain. [ABSTRACT FROM AUTHOR]
Copyright of Acta Crystallographica: Section D (Wiley-Blackwell) is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Structure of cytochrome c<subscript>7</subscript> from Desulfuromonas acetoxidans at 1.9 Å resolution.
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  Data: <searchLink fieldCode="AR" term="%22Czjzek%2C+Mirjam%22">Czjzek, Mirjam</searchLink><relatesTo>1</relatesTo><i> czjzek@afmb.cnrs-mrs.fr</i><br /><searchLink fieldCode="AR" term="%22Arnoux%2C+Pascal%22">Arnoux, Pascal</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Haser%2C+Richard%22">Haser, Richard</searchLink><relatesTo>2</relatesTo><br /><searchLink fieldCode="AR" term="%22Shepardc%2C+William%22">Shepardc, William</searchLink><relatesTo>3</relatesTo>
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  Data: <searchLink fieldCode="JN" term="%22Acta+Crystallographica%3A+Section+D+%28Wiley-Blackwell%29%22">Acta Crystallographica: Section D (Wiley-Blackwell)</searchLink>. May2001, Vol. 57 Issue 5, p670-678. 9p.
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  Data: <searchLink fieldCode="DE" term="%22Cytochromes%22">Cytochromes</searchLink><br /><searchLink fieldCode="DE" term="%22Bacteria%22">Bacteria</searchLink><br /><searchLink fieldCode="DE" term="%22Proteins%22">Proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Metals%22">Metals</searchLink><br /><searchLink fieldCode="DE" term="%22Biotechnology%22">Biotechnology</searchLink><br /><searchLink fieldCode="DE" term="%22Porphyrins%22">Porphyrins</searchLink>
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  Label: Abstract
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  Data: Multihaem cytochromes play a key role in electron-transport reactions in the periplasm of sulfate- and sulfur-reducing bacteria. The redox proteins grouped in the c3 superfamily also display metal-reducing activities, which make them interesting biotechnological tools. The crystal structure of the fully oxidized cytochrome c7 from Desulfuromonas acetoxidans has been solved by combined molecular- replacement and MAD methods. The structure has been refined at 1.9 Å resolution to an R value of 19.1% (Rfree = 24.3%) and includes three haems and 116 water molecules. The protein displays the cytochrome c3 fold in a highly minimized form, while haem 2 and the surrounding protein environment are missing. The geometry of haem packing and of the haem axial ligands and propionates are described and compared with that of c3 cytochromes. The crystal structure is compared with the solution structure recently obtained by NMR methods and with its homologue cytochromes of the c3 superfamily. Comparison of the high number of available structures makes it possible to analyze the structural role of the few highly conserved residues, in addition to the cysteines and histidines that link the porphyrin rings and the Fe atoms to the protein chain. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Acta Crystallographica: Section D (Wiley-Blackwell) is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1107/S0907444901003481
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        Text: English
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      – TitleFull: Structure of cytochrome c7 from Desulfuromonas acetoxidans at 1.9 Å resolution.
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              Text: May2001
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              Y: 2001
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