6VQK
Mammalian V-ATPase from rat brain collar and peripheral stalks rotational state 3 (from focused refinement)
6VQK の概要
エントリーDOI | 10.2210/pdb6vqk/pdb |
EMDBエントリー | 21353 |
分子名称 | V-type proton ATPase subunit C 1, V-type proton ATPase subunit E 1, V-type proton ATPase subunit G, ... (4 entities in total) |
機能のキーワード | membrane protein complex, rotary atpase, proton transport |
由来する生物種 | Rattus norvegicus (Rat) 詳細 |
タンパク質・核酸の鎖数 | 8 |
化学式量合計 | 259961.68 |
構造登録者 | |
主引用文献 | Abbas, Y.M.,Wu, D.,Bueler, S.A.,Robinson, C.V.,Rubinstein, J.L. Structure of V-ATPase from the mammalian brain. Science, 367:1240-1246, 2020 Cited by PubMed Abstract: In neurons, the loading of neurotransmitters into synaptic vesicles uses energy from proton-pumping vesicular- or vacuolar-type adenosine triphosphatases (V-ATPases). These membrane protein complexes possess numerous subunit isoforms, which complicates their analysis. We isolated homogeneous rat brain V-ATPase through its interaction with SidK, a effector protein. Cryo-electron microscopy allowed the construction of an atomic model, defining the enzyme's ATP:proton ratio as 3:10 and revealing a homolog of yeast subunit f in the membrane region, which we tentatively identify as RNAseK. The c ring encloses the transmembrane anchors for cleaved ATP6AP1/Ac45 and ATP6AP2/PRR, the latter of which is the (pro)renin receptor that, in other contexts, is involved in both Wnt signaling and the renin-angiotensin system that regulates blood pressure. This structure shows how ATP6AP1/Ac45 and ATP6AP2/PRR enable assembly of the enzyme's catalytic and membrane regions. PubMed: 32165585DOI: 10.1126/science.aaz2924 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (5.7 Å) |
構造検証レポート
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