Structural similarity of cytochrome c 2 from Rhodopseudomonas viridis to mitochondrial cytochromes c revealed by its crystal structure at 2.7 Å resolution

FEBS Letters

Ezoe, Toshihide¹  Uno, Atsushi¹  Miki, Miyako²  Sogabe, Satoshi³  Saeda, Masahiko¹  Kasai, Nobutami¹  Miki, Kunio³ 

[1] Department of Applied Chemistry, Faculty of Engineering, Osaka University, Yamadaoka, Suita, Osaka 565, Japan;Institute of Scientific and Industrial Research, Osaka University, Mihogaoka, Ibaraki, Osaka 567, Japan;Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Nagatsuta, Midori-ku, Yokohama 227, Japan

关键词: Cytochrome c 2;    Crystal structure;    X-ray crystallography;    Rhodopseudomonas viridis;   

DOI  :  10.1016/0014-5793(94)00389-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The crystal structure of cytochrome c ₂ from Rhodopseudomonas viridis has been refined using molecular dynamics and restrained least-squares methods to a crystallographic R-factor of 0.216 at 2.7 Å resolution. A structural comparison between Rps. viridis cytochrome c ₂ and the other bacterial cytochromes C ₂ or mitochondrial cytochromes c indicates that the overall protein foldings are very similar to each other with the exception of the surface loop and terminal region of the polypeptide chain. However, the position and hydrogen-bond pattern of the evolutionarily conserved water molecule buried within the heme binding pocket in Rps. viridis cytochrome c ₂ are common to those in the mitochondrial cytochromes c. This fact indicates that Rps. viridis cytochrome c ₂ is structurally more similar to mitochondrial cytochromes c than to the other bacterial cytochromes c ₂.

【 授权许可】

Unknown