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-Structure paper
タイトル | Coordinated conformational changes in the V complex during V-ATPase reversible dissociation. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 29, Issue 5, Page 430-439, Year 2022 |
掲載日 | 2022年4月25日 |
著者 | Thamiya Vasanthakumar / Kristine A Keon / Stephanie A Bueler / Michael C Jaskolka / John L Rubinstein / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Struct Mol Biol / PubMed:35469063 |
手法 | EM (単粒子) |
解像度 | 3.3 - 3.8 Å |
構造データ | EMDB-25996, PDB-7tmm: EMDB-25997, PDB-7tmo: EMDB-25998, PDB-7tmp: EMDB-25999, PDB-7tmq: EMDB-26000, PDB-7tmr: EMDB-26001, PDB-7tms: EMDB-26002, PDB-7tmt: |
化合物 | ChemComp-ADP: ChemComp-ATP: ChemComp-MG: |
由来 |
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キーワード | HYDROLASE / V-ATPase / MEMBRANE PROTEIN |