1hh5
From Proteopedia
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[[Category: multiheme cytochrome]] | [[Category: multiheme cytochrome]] | ||
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Revision as of 13:31, 30 October 2007
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CYTOCHROME C7 FROM DESULFUROMONAS ACETOXIDANS
Overview
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 A resolution to an R value of 19.1%, (R(free) = 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, ... [(full description)]
About this Structure
1HH5 is a [Single protein] structure of sequence from [Desulfuromonas acetoxidans] with HEC as [ligand]. Structure known Active Sites: HC1, HC2 and HC3. Full crystallographic information is available from [OCA].
Reference
Structure of cytochrome c7 from Desulfuromonas acetoxidans at 1.9 A resolution., Czjzek M, Arnoux P, Haser R, Shepard W, Acta Crystallogr D Biol Crystallogr. 2001 May;57(Pt 5):670-8. Epub 2001, Apr 24. PMID:11320307
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