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7UWC

Citrus V-ATPase State 2, H in contact with subunit a

これはPDB形式変換不可エントリーです。
7UWC の概要
エントリーDOI10.2210/pdb7uwc/pdb
EMDBエントリー26828
分子名称V-type proton ATPase subunit H, V-type proton ATPase subunit AP1 fragment, V-type proton ATPase subunit c", ... (15 entities in total)
機能のキーワードv-atpase, rotary atpase, complex, membrane protein
由来する生物種Citrus limon
詳細
タンパク質・核酸の鎖数31
化学式量合計937231.60
構造登録者
Keon, K.A.,Abdelaziz, R.A.,Schulze, W.X.,Schumacher, K.,Rubinstein, J.L. (登録日: 2022-05-03, 公開日: 2022-07-06, 最終更新日: 2024-01-17)
主引用文献Tan, Y.Z.,Keon, K.A.,Abdelaziz, R.,Imming, P.,Schulze, W.,Schumacher, K.,Rubinstein, J.L.
Structure of V-ATPase from citrus fruit.
Structure, 30:1403-, 2022
Cited by
PubMed Abstract: We used the Legionella pneumophila effector SidK to affinity purify the endogenous vacuolar-type ATPases (V-ATPases) from lemon fruit. The preparation was sufficient for cryoelectron microscopy, allowing structure determination of the enzyme in two rotational states. The structure defines the ATP:H ratio of the enzyme, demonstrating that it can establish a maximum ΔpH of ∼3, which is insufficient to maintain the low pH observed in the vacuoles of juice sac cells in lemons and other citrus fruit. Compared with yeast and mammalian enzymes, the membrane region of the plant V-ATPase lacks subunit f and possesses an unusual configuration of transmembrane α helices. Subunit H, which inhibits ATP hydrolysis in the isolated catalytic region of V-ATPase, adopts two different conformations in the intact complex, hinting at a role in modulating activity in the intact enzyme.
PubMed: 36041457
DOI: 10.1016/j.str.2022.07.006
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (4 Å)
構造検証レポート
Validation report summary of 7uwc
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2025-06-18に公開中

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