1RYC

CYTOCHROME C PEROXIDASE W191G FROM SACCHAROMYCES CEREVISIAE

1RYC の概要

• エントリーDOI: 10.2210/pdb1ryc/pdb
• 分子名称: CYTOCHROME C PEROXIDASE, PROTOPORPHYRIN IX CONTAINING FE, BENZIMIDAZOLE, ... (4 entities in total)
• 機能のキーワード: oxidoreductase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Mitochondrion matrix: P00431
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34192.88

構造登録者

Fitzgerald, M.M.,Musah, R.,Mcree, D.E.,Goodin, D.B. (登録日: 1996-05-10, 公開日: 1996-11-08, 最終更新日: 2024-02-14)

主引用文献

Fitzgerald, M.M.,Musah, R.A.,McRee, D.E.,Goodin, D.B.
A ligand-gated, hinged loop rearrangement opens a channel to a buried artificial protein cavity.
Nat.Struct.Biol., 3:626-631, 1996

PubMed Abstract: Conformational changes that gate the access of substrates or ligands to an active site are important features of enzyme function. In this report, we describe an unusual example of a structural rearrangement near a buried artificial cavity in cytochrome c peroxidase that occurs on binding protonated benzimidazole. A hinged main-chain rotation at two residues (Pro 190 and Asn 195) results in a surface loop rearrangement that opens a large solvent-accessible channel for the entry of ligands to an otherwise inaccessible binding site. The trapping of this alternate conformational state provides a unique view of the extent to which protein dynamics can allow small molecule penetration into buried protein cavities.

PubMed: 8673607
DOI: 10.1038/nsb0796-626

実験手法

X-RAY DIFFRACTION (1.8 Å)