2CY3

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

Replaces:  1CY3

Summary for 2CY3

• Entry DOI: 10.2210/pdb2cy3/pdb
• Descriptor: CYTOCHROME C3, HEME C (3 entities in total)
• Functional Keywords: electron transport (heme protein)
• Biological source: Desulfomicrobium norvegicum
• Cellular location: Periplasm: P00136
• Total number of polymer chains: 1
• Total formula weight: 15122.45

Authors

Czjzek, M.,Payan, F.,Haser, R. (deposition date: 1994-07-01, release date: 1994-10-15, Last modification date: 2024-11-20)

Primary citation

Czjzek, M.,Payan, F.,Guerlesquin, F.,Bruschi, M.,Haser, R.
Crystal structure of cytochrome c3 from Desulfovibrio desulfuricans Norway at 1.7 A resolution.
J.Mol.Biol., 243:653-667, 1994

PubMed Abstract: 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.

PubMed: 7966289
DOI: 10.1016/0022-2836(94)90039-6

Experimental method

X-RAY DIFFRACTION (1.7 Å)