3CYT

REDOX CONFORMATION CHANGES IN REFINED TUNA CYTOCHROME C

「1CYT」から置き換えられました

3CYT の概要

• エントリーDOI: 10.2210/pdb3cyt/pdb
• 分子名称: CYTOCHROME C, 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: Thunnus alalunga (albacore)
• 細胞内の位置: Mitochondrion intermembrane space: P81459
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24069.23

構造登録者

Takano, T. (登録日: 1980-07-01, 公開日: 1980-09-16, 最終更新日: 2024-10-23)

主引用文献

Takano, T.,Dickerson, R.E.
Redox conformation changes in refined tuna cytochrome c.
Proc.Natl.Acad.Sci.USA, 77:6371-6375, 1980

PubMed Abstract: Tuna ferrocytochrome c and ferricytochrome c have been refined independently at high resolution (1.5 A and 1.8 A) to crystallographic residual errors of 17.3% and 20.8%, respectively. Small but significant conformational differences are seen surrounding a buried water molecule that is hydrogen bonded to Asn-52, Tyr-67, and Thr-78. In the oxidized state, this water molecule is 1.0 A closer to the heme and the heme has moved 0.15 A out of its heme crevice; both changes lead to a more polar microenvironment for the heme. Chemical modification studies, patterns of evolutionary conservatism, structural differences in bacterial cytochromes, and x-ray studies all agree that the "active site" for cytochrome c is bounded by lysines 8, 13,27, 72, 79, 86, and 87 (thus containing the evolutionary conservative 72-87 loop) and has the buried water molecule just below its surface and the opening of the heme crevice slightly to one side.

PubMed: 6256733
DOI: 10.1073/pnas.77.11.6371

実験手法

X-RAY DIFFRACTION (1.8 Å)