2CY3

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

「1CY3」から置き換えられました

2CY3 の概要

• エントリーDOI: 10.2210/pdb2cy3/pdb
• 分子名称: CYTOCHROME C3, HEME C (3 entities in total)
• 機能のキーワード: electron transport (heme protein)
• 由来する生物種: Desulfomicrobium norvegicum
• 細胞内の位置: Periplasm: P00136
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15122.45

構造登録者

Czjzek, M.,Payan, F.,Haser, R. (登録日: 1994-07-01, 公開日: 1994-10-15, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.7 Å)