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1E79

Bovine F1-ATPase inhibited by DCCD (dicyclohexylcarbodiimide)

1E79 の概要
エントリーDOI10.2210/pdb1e79/pdb
関連するPDBエントリー1BMF 1COW 1E1Q 1E1R 1EFR 1NBM 1QO1
分子名称ATP SYNTHASE ALPHA CHAIN HEART ISOFORM, DICYCLOHEXYLUREA, SULFATE ION, ... (12 entities in total)
機能のキーワードatp phosphorylase, atp phosphorylase (h+ transporting), f1fo atp synthase, central stalk, hydrolase
由来する生物種BOS TAURUS (BOVINE)
詳細
細胞内の位置Mitochondrion inner membrane (By similarity): P19483
Mitochondrion: P00829 P05631 P05630 P05632
タンパク質・核酸の鎖数9
化学式量合計374930.30
構造登録者
Gibbons, C.,Montgomery, M.G.,Leslie, A.G.W.,Walker, J.E. (登録日: 2000-08-25, 公開日: 2000-11-03, 最終更新日: 2024-10-09)
主引用文献Gibbons, C.,Montgomery, M.G.,Leslie, A.G.W.,Walker, J.E.
The Structure of the Central Stalk in Bovine F(1)-ATPase at 2.4 A Resolution.
Nat.Struct.Biol., 7:1055-, 2000
Cited by
PubMed Abstract: The central stalk in ATP synthase, made of gamma, delta and epsilon subunits in the mitochondrial enzyme, is the key rotary element in the enzyme's catalytic mechanism. The gamma subunit penetrates the catalytic (alpha beta)(3) domain and protrudes beneath it, interacting with a ring of c subunits in the membrane that drives rotation of the stalk during ATP synthesis. In other crystals of F(1)-ATPase, the protrusion was disordered, but with crystals of F(1)-ATPase inhibited with dicyclohexylcarbodiimide, the complete structure was revealed. The delta and epsilon subunits interact with a Rossmann fold in the gamma subunit, forming a foot. In ATP synthase, this foot interacts with the c-ring and couples the transmembrane proton motive force to catalysis in the (alpha beta)(3) domain.
PubMed: 11062563
DOI: 10.1038/80981
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.4 Å)
構造検証レポート
Validation report summary of 1e79
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-01-28に公開中

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