7TMT

V-ATPase from Saccharomyces cerevisiae, State 3

これはPDB形式変換不可エントリーです。

7TMT の概要

• エントリーDOI: 10.2210/pdb7tmt/pdb
• EMDBエントリー: 26002
• 分子名称: H(+)-transporting two-sector ATPase, V0 assembly protein 1, V-type proton ATPase subunit c'', ... (17 entities in total)
• 機能のキーワード: v-atpase, membrane protein
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• タンパク質・核酸の鎖数: 31
• 化学式量合計: 989858.11

構造登録者

Vasanthakumar, T.,Keon, K.A.,Bueler, S.A.,Jaskolka, M.C.,Rubinstein, J.L. (登録日: 2022-01-20, 公開日: 2022-04-20, 最終更新日: 2025-05-28)

主引用文献

Vasanthakumar, T.,Keon, K.A.,Bueler, S.A.,Jaskolka, M.C.,Rubinstein, J.L.
Coordinated conformational changes in the V 1 complex during V-ATPase reversible dissociation.
Nat.Struct.Mol.Biol., 29:430-439, 2022

PubMed Abstract: Vacuolar-type ATPases (V-ATPases) are rotary enzymes that acidify intracellular compartments in eukaryotic cells. These multi-subunit complexes consist of a cytoplasmic V region that hydrolyzes ATP and a membrane-embedded V region that transports protons. V-ATPase activity is regulated by reversible dissociation of the two regions, with the isolated V and V complexes becoming autoinhibited on disassembly and subunit C subsequently detaching from V. In yeast, assembly of the V and V regions is mediated by the regulator of the ATPase of vacuoles and endosomes (RAVE) complex through an unknown mechanism. We used cryogenic-electron microscopy of yeast V-ATPase to determine structures of the intact enzyme, the dissociated but complete V complex and the V complex lacking subunit C. On separation, V undergoes a dramatic conformational rearrangement, with its rotational state becoming incompatible for reassembly with V. Loss of subunit C allows V to match the rotational state of V, suggesting how RAVE could reassemble V and V by recruiting subunit C.

PubMed: 35469063
DOI: 10.1038/s41594-022-00757-z

実験手法

ELECTRON MICROSCOPY (3.8 Å)