2cy3

From Proteopedia

Revision as of 07:12, 21 November 2007

CRYSTAL STRUCTURE OF CYTOCHROME C3 FROM DESULFOVIBRIO DESULFURICANS NORWAY AT 1.7 ANGSTROMS RESOLUTION

Overview

The crystal structure of cytochrome c3 (M(r) 13,000) from Desulfovibrio, desulfuricans (118 residues, four heme groups) has been, crystallographically refined to 1.7 A resolution using a simulated, annealing method, based on the structure-model at 2.5 A resolution, already published. The final R-factor for 10,549 reflections was 0.198, covering the range from 5.5 to 1.7 A resolution. The individual, temperature factors were refined for a total of 1059 protein atoms, together with 126 bound solvent molecules. The structure has been analyzed, with respect to its detailed conformational properties, secondary, structure features, temperature factor behaviour, bound solvent sites and, heme geometry and ligation. The characteristic secondary structures of the, polypeptide chain of this molecule are one extended alpha-helix, a short, beta-strand and 13 reverse turns. The four heme groups are located in, different structural environments, all highly exposed to solvent. The, particular structural features of the heme environments are compared to, the four hemes of the cytochrome c3 from Desulfovibrio vulgaris Miyazaki.

About this Structure

2CY3 is a Single protein structure of sequence from Desulfovibrio desulfuricans with HEM as ligand. This structure superseeds the now removed PDB entry 1CY3. Full crystallographic information is available from OCA.

Reference

Crystal structure of cytochrome c3 from Desulfovibrio desulfuricans Norway at 1.7 A resolution., Czjzek M, Payan F, Guerlesquin F, Bruschi M, Haser R, J Mol Biol. 1994 Nov 4;243(4):653-67. PMID:7966289

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