5GAR

Thermus thermophilus V/A-ATPase, conformation 1

5GAR の概要

• エントリーDOI: 10.2210/pdb5gar/pdb
• 関連するPDBエントリー: 5GAS 5I1M
• EMDBエントリー: 8016 8017 8070
• 分子名称: V-type ATP synthase alpha chain, V-type ATP synthase beta chain, V-type ATP synthase subunit E, ... (9 entities in total)
• 機能のキーワード: v/a-atpase, v-atpase, a-atpase, thermus thermophilus, rotary atpase, membrane protein, hydrolase
• 由来する生物種: Thermus thermophilus; 詳細
• タンパク質・核酸の鎖数: 26
• 化学式量合計: 668423.74

構造登録者

Schep, D.G.,Zhao, J.,Rubinstein, J.L. (登録日: 2016-02-05, 公開日: 2016-03-09, 最終更新日: 2024-03-06)

主引用文献

Schep, D.G.,Zhao, J.,Rubinstein, J.L.
Models for the a subunits of the Thermus thermophilus V/A-ATPase and Saccharomyces cerevisiae V-ATPase enzymes by cryo-EM and evolutionary covariance.
Proc.Natl.Acad.Sci.USA, 113:3245-3250, 2016

PubMed Abstract: Rotary ATPases couple ATP synthesis or hydrolysis to proton translocation across a membrane. However, understanding proton translocation has been hampered by a lack of structural information for the membrane-embedded a subunit. The V/A-ATPase from the eubacterium Thermus thermophilus is similar in structure to the eukaryotic V-ATPase but has a simpler subunit composition and functions in vivo to synthesize ATP rather than pump protons. We determined the T. thermophilus V/A-ATPase structure by cryo-EM at 6.4 Å resolution. Evolutionary covariance analysis allowed tracing of the a subunit sequence within the map, providing a complete model of the rotary ATPase. Comparing the membrane-embedded regions of the T. thermophilus V/A-ATPase and eukaryotic V-ATPase from Saccharomyces cerevisiae allowed identification of the α-helices that belong to the a subunit and revealed the existence of previously unknown subunits in the eukaryotic enzyme. Subsequent evolutionary covariance analysis enabled construction of a model of the a subunit in the S. cerevisae V-ATPase that explains numerous biochemical studies of that enzyme. Comparing the two a subunit structures determined here with a structure of the distantly related a subunit from the bovine F-type ATP synthase revealed a conserved pattern of residues, suggesting a common mechanism for proton transport in all rotary ATPases.

PubMed: 26951669
DOI: 10.1073/pnas.1521990113

実験手法

ELECTRON MICROSCOPY (6.4 Å)