1hh5
From Proteopedia
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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, 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.
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
Page seeded by OCA on Mon Nov 5 16:36:10 2007
