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-Structure paper
タイトル | Structure and conformational plasticity of the intact V/A-type ATPase. |
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ジャーナル・号・ページ | Science, Vol. 365, Issue 6455, Year 2019 |
掲載日 | 2019年8月23日 |
著者 | Long Zhou / Leonid A Sazanov / |
PubMed 要旨 | V (vacuolar)/A (archaeal)-type adenosine triphosphatases (ATPases), found in archaea and eubacteria, couple ATP hydrolysis or synthesis to proton translocation across the plasma membrane using the ...V (vacuolar)/A (archaeal)-type adenosine triphosphatases (ATPases), found in archaea and eubacteria, couple ATP hydrolysis or synthesis to proton translocation across the plasma membrane using the rotary-catalysis mechanism. They belong to the V-type ATPase family, which differs from the mitochondrial/chloroplast F-type ATP synthases in overall architecture. We solved cryo-electron microscopy structures of the intact V/A-ATPase, reconstituted into lipid nanodiscs, in three rotational states and two substates. These structures indicate substantial flexibility between V and V in a working enzyme, which results from mechanical competition between central shaft rotation and resistance from the peripheral stalks. We also describe details of adenosine diphosphate inhibition release, V-V torque transmission, and proton translocation, which are relevant for the entire V-type ATPase family. |
リンク | Science / PubMed:31439765 |
手法 | EM (単粒子) |
解像度 | 3.25 - 4.3 Å |
構造データ | EMDB-4640, PDB-6qum: EMDB-4699, PDB-6r0w: EMDB-4700, PDB-6r0y: |
化合物 | ChemComp-MG: ChemComp-ADP: |
由来 |
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キーワード | MEMBRANE PROTEIN / ATP hydrolysis/synthesis / proton translocation / rotary catalysis |