V-type ATP synthase subunit I, N-terminal / Vacuolar ATPase subunit I, N-terminal proximal lobe / Vacuolar ATPase Subunit I N-terminal proximal lobe / V-type ATPase subunit I, N-terminal domain / ATPase, V0 complex, c subunit / : / Vacuolar (H+)-ATPase G subunit / V-ATPase proteolipid subunit / ATPase, V0 complex, c/d subunit / V-type ATPase subunit C/d ...V-type ATP synthase subunit I, N-terminal / Vacuolar ATPase subunit I, N-terminal proximal lobe / Vacuolar ATPase Subunit I N-terminal proximal lobe / V-type ATPase subunit I, N-terminal domain / ATPase, V0 complex, c subunit / : / Vacuolar (H+)-ATPase G subunit / V-ATPase proteolipid subunit / ATPase, V0 complex, c/d subunit / V-type ATPase subunit C/d / V-type ATP synthase subunit c/d subunit superfamily / V-type ATP synthase c/d subunit, domain 3 superfamily / ATP synthase (C/AC39) subunit / V-type ATPase, V0 complex, 116kDa subunit family / V-type ATPase 116kDa subunit family / V-type ATPase subunit E / V-type ATPase subunit E, C-terminal domain superfamily / ATP synthase (E/31 kDa) subunit / V-ATPase proteolipid subunit C-like domain / F/V-ATP synthase subunit C superfamily / ATP synthase subunit C 類似検索 - ドメイン・相同性
V-type ATP synthase subunit E / V-type ATP synthase subunit C / V-type ATP synthase, subunit (VAPC-THERM) / V-type ATP synthase subunit I / V-type ATP synthase, subunit K 類似検索 - 構成要素
Japan Agency for Medical Research and Development (AMED)
JP17am0101001
日本
Ministry of Education, Culture, Sports, Science and Technology (Japan)
12024046
日本
引用
ジャーナル: Elife / 年: 2020 タイトル: Mechanical inhibition of isolated V from V/A-ATPase for proton conductance. 著者: Jun-Ichi Kishikawa / Atsuko Nakanishi / Aya Furuta / Takayuki Kato / Keiichi Namba / Masatada Tamakoshi / Kaoru Mitsuoka / Ken Yokoyama / 要旨: V-ATPase is an energy converting enzyme, coupling ATP hydrolysis/synthesis in the hydrophilic V domain, with proton flow through the V membrane domain, via rotation of the central rotor complex ...V-ATPase is an energy converting enzyme, coupling ATP hydrolysis/synthesis in the hydrophilic V domain, with proton flow through the V membrane domain, via rotation of the central rotor complex relative to the surrounding stator apparatus. Upon dissociation from the V domain, the V domain of the eukaryotic V-ATPase can adopt a physiologically relevant auto-inhibited form in which proton conductance through the V domain is prevented, however the molecular mechanism of this inhibition is not fully understood. Using cryo-electron microscopy, we determined the structure of both the V/A-ATPase and isolated V at near-atomic resolution, respectively. These structures clarify how the isolated V domain adopts the auto-inhibited form and how the complex prevents formation of the inhibited V form.
N: V-type ATP synthase subunit I O: V-type ATP synthase, subunit K P: V-type ATP synthase, subunit K Q: V-type ATP synthase, subunit K R: V-type ATP synthase, subunit K S: V-type ATP synthase, subunit K T: V-type ATP synthase, subunit K U: V-type ATP synthase, subunit K V: V-type ATP synthase, subunit K W: V-type ATP synthase, subunit K X: V-type ATP synthase, subunit K Y: V-type ATP synthase, subunit K Z: V-type ATP synthase, subunit K M: V-type ATP synthase subunit C K: V-type ATP synthase, subunit (VAPC-THERM) L: V-type ATP synthase subunit E
名称: Membrane-embedded Vo domain / タイプ: COMPLEX / 詳細: V/A-type ATPase from Thermus thermophilus / Entity ID: all / 由来: NATURAL
分子量
ID
Entity assembly-ID
値 (°)
実験値
1
1
0.650MDa
NO
2
1
0.26MDa
NO
由来(天然)
生物種: Thermus thermophilus HB8 (バクテリア)
緩衝液
pH: 8
緩衝液成分
ID
濃度
名称
式
Buffer-ID
1
50mM
Tris-HCl
1
2
150mM
SodiumChloride
NaCl
1
試料
濃度: 3 mg/ml / 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES 詳細: The sample was purified from cell membrane of Thermus thermophilus and incorporated into nanodisc.