1CYC

THE CRYSTAL STRUCTURE OF BONITO (KATSUO) FERROCYTOCHROME C AT 2.3 ANGSTROMS RESOLUTION. II. STRUCTURE AND FUNCTION

1CYC の概要

• エントリーDOI: 10.2210/pdb1cyc/pdb
• 分子名称: FERROCYTOCHROME C, HEME C (3 entities in total)
• 機能のキーワード: electron transport
• 由来する生物種: Katsuwonus pelamis (skipjack tuna)
• 細胞内の位置: Mitochondrion intermembrane space: P00025
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24045.21

構造登録者

Tanaka, N.,Yamane, T.,Tsukihara, T.,Ashida, T.,Kakudo, M. (登録日: 1976-08-01, 公開日: 1976-10-06, 最終更新日: 2024-12-25)

主引用文献

Tanaka, N.,Yamane, T.,Tsukihara, T.,Ashida, T.,Kakudo, M.
The crystal structure of bonito (katsuo) ferrocytochrome c at 2.3 A resolution. II. Structure and function.
J.Biochem.(Tokyo), 77:147-162, 1975

PubMed Abstract: The structure analysis of bonito heart ferrocytochrome c was carried out at 2.3 A resolution by X-ray diffraction, and a Kendrew-type skeletal model was built up. This molecule has an overall egg shape, 35 A in height, 30 A in width and 23 A in thickness; the 5th ligand of the heme iron atom is the N-epsilon atom of the His-18 imidazole ring and the 6th is the Met-80 sulfur atom. Distinct alpha-helix regions are found between the N-terminus and reside 11, between 60 and 69, and between 90 and the C-terminus. The most distinct difference between the conformation of the present molecule and that of the horse oxidized molecule is the location of the Phe-82 phenyl ring. In the present reduced molecule, the phyenyl ring is in closer contact with the iron atom and gives influences on the character of the iron atom. Inside the molecule, at the lower part of the heme pocket, there is an extended hydrogen bond network including the propionic acid residues of the heme group. Both Phe-82 and the hydrogen bond network may play a key role in the function of this molecule.

PubMed: 166072

実験手法

X-RAY DIFFRACTION (2.3 Å)