2cdv
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(New page: 200px<br /><applet load="2cdv" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cdv, resolution 1.8Å" /> '''REFINED STRUCTURE OF ...)
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Revision as of 06:58, 21 November 2007
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REFINED STRUCTURE OF CYTOCHROME C3 AT 1.8 ANGSTROMS RESOLUTION
Overview
The structure of cytochrome c3 from the sulfate-reducing bacterium, Desulfovibrio vulgaris Miyazaki has been successfully refined at 1.8 A, resolution. The crystallographic R factor is 0.176 for 9907 significant, reflections. The isotropic temperature factors of individual atoms were, refined and a total of 47 water molecules located on the difference map, were incorporated in the refinement. The four heme groups are closely, packed, with adjacent pairs of heme planes being nearly perpendicular to, each other. The fifth and the sixth ligands of the heme iron atoms are, histidine residues with N epsilon 2-Fe distances ranging from 1.88 A to, 2.12 A. The histidine co-ordination to the heme iron is different for each, heme group. The heme groups are all highly exposed to solvent, although, the actual regions exposed differ among the hemes. The four heme groups, are located in different environments, and the heme planes are deformed, from planarity. The differences in the heme structures and their, environments indicate that the four heme groups are non-equivalent. The, chemical as well as the physical properties of cytochrome c3 should be, interpreted in terms of the structural non-equivalence of the heme groups., The characteristic secondary structural non-equivalence of the heme, groups. The characteristic secondary structures of the polypeptide chain, of this molecule are three short alpha-helices, two short beta-strands and, ten reverse turns.
About this Structure
2CDV is a Single protein structure of sequence from Desulfovibrio vulgaris with HEM as ligand. This structure superseeds the now removed PDB entry 1CDV. Full crystallographic information is available from OCA.
Reference
Refined structure of cytochrome c3 at 1.8 A resolution., Higuchi Y, Kusunoki M, Matsuura Y, Yasuoka N, Kakudo M, J Mol Biol. 1984 Jan 5;172(1):109-39. PMID:6319712
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