登録情報 データベース : EMDB / ID : EMD-26828 ダウンロードとリンクタイトル Citrus V-ATPase State 2, H in contact with subunit a マップデータCitrus V-ATPase State 2, H in contact with subunit a 詳細 試料 詳細 キーワード V-ATPase / rotary ATPase / complex / MEMBRANE PROTEIN機能・相同性 機能・相同性情報分子機能 ドメイン・相同性 構成要素
proton-transporting V-type ATPase, V1 domain / proton-transporting V-type ATPase, V0 domain / proton-transporting two-sector ATPase complex, catalytic domain / plasma membrane proton-transporting V-type ATPase complex / vacuolar proton-transporting V-type ATPase, V0 domain / vacuolar proton-transporting V-type ATPase, V1 domain / vacuolar transport / plant-type vacuole / proton-transporting V-type ATPase complex / vacuolar proton-transporting V-type ATPase complex ... proton-transporting V-type ATPase, V1 domain / proton-transporting V-type ATPase, V0 domain / proton-transporting two-sector ATPase complex, catalytic domain / plasma membrane proton-transporting V-type ATPase complex / vacuolar proton-transporting V-type ATPase, V0 domain / vacuolar proton-transporting V-type ATPase, V1 domain / vacuolar transport / plant-type vacuole / proton-transporting V-type ATPase complex / vacuolar proton-transporting V-type ATPase complex / vacuole / vacuolar acidification / vacuolar membrane / ATP metabolic process / H+-transporting two-sector ATPase / phagocytic vesicle / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / transmembrane transport / ATPase binding / early endosome / lysosomal membrane / ATP hydrolysis activity / ATP binding / membrane 類似検索 - 分子機能 ATPase, V1 complex, subunit A / ATPase, V1 complex, subunit C / Vacuolar ATP synthase subunit C superfamily / V-ATPase subunit C / Vacuolar (H+)-ATPase G subunit / Vacuolar (H+)-ATPase G subunit / ATPase, V1 complex, subunit B / ATPase, V1 complex, subunit F, eukaryotic / ATPase, V0 complex, subunit e1/e2 / ATP synthase subunit H ... ATPase, V1 complex, subunit A / ATPase, V1 complex, subunit C / Vacuolar ATP synthase subunit C superfamily / V-ATPase subunit C / Vacuolar (H+)-ATPase G subunit / Vacuolar (H+)-ATPase G subunit / ATPase, V1 complex, subunit B / ATPase, V1 complex, subunit F, eukaryotic / ATPase, V0 complex, subunit e1/e2 / ATP synthase subunit H / ATPase, V0 complex, subunit d / V-ATPase proteolipid subunit C, eukaryotic / ATPase, V0 complex, subunit 116kDa, eukaryotic / 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 / ATPase, V1 complex, subunit D / ATPase, V1 complex, subunit F / ATPase, V1 complex, subunit F superfamily / ATP synthase subunit D / ATP synthase (F/14-kDa) subunit / V-type ATP synthase regulatory subunit B/beta / V-type ATP synthase catalytic alpha chain / ATPsynthase alpha/beta subunit, N-terminal extension / ATPsynthase alpha/beta subunit N-term extension / V-ATPase proteolipid subunit C-like domain / F/V-ATP synthase subunit C superfamily / ATP synthase subunit C / ATPase, F1/V1 complex, beta/alpha subunit, C-terminal / ATP synthase subunit alpha, N-terminal domain-like superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain superfamily / ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain / ATP synthase alpha/beta family, beta-barrel domain / ATPase, alpha/beta subunit, nucleotide-binding domain, active site / ATP synthase alpha and beta subunits signature. / ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain / ATP synthase alpha/beta family, nucleotide-binding domain / P-loop containing nucleoside triphosphate hydrolase 類似検索 - ドメイン・相同性 V-type proton ATPase subunit G / V-type proton ATPase subunit F / V-type proton ATPase subunit e1 / V-type proton ATPase subunit D / Vacuolar proton pump subunit B / V-type proton ATPase subunit / V-type proton ATPase subunit C / V-type proton ATPase subunit c1 / Vacuolar membrane ATPase subunit c / V-type proton ATPase subunit E ... V-type proton ATPase subunit G / V-type proton ATPase subunit F / V-type proton ATPase subunit e1 / V-type proton ATPase subunit D / Vacuolar proton pump subunit B / V-type proton ATPase subunit / V-type proton ATPase subunit C / V-type proton ATPase subunit c1 / Vacuolar membrane ATPase subunit c / V-type proton ATPase subunit E / V-type proton ATPase catalytic subunit A / V-type proton ATPase subunit a 類似検索 - 構成要素生物種 Citrus limon (植物)手法 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度 : 4.0 Å 詳細 データ登録者Tan YZ / Rubinstein JL 資金援助 カナダ, 1件 詳細 詳細を隠すOrganization Grant number 国 Natural Sciences and Engineering Research Council (NSERC, Canada) カナダ
引用ジャーナル : Structure / 年 : 2022タイトル : Structure of V-ATPase from citrus fruit.著者 : Yong Zi Tan / Kristine A Keon / Rana Abdelaziz / Peter Imming / Waltraud Schulze / Karin Schumacher / John L Rubinstein / 要旨 : We used the Legionella pneumophila effector SidK to affinity purify the endogenous vacuolar-type ATPases (V-ATPases) from lemon fruit. The preparation was sufficient for cryoelectron microscopy, ... We used the Legionella pneumophila effector SidK to affinity purify the endogenous vacuolar-type ATPases (V-ATPases) from lemon fruit. The preparation was sufficient for cryoelectron microscopy, allowing structure determination of the enzyme in two rotational states. The structure defines the ATP:H ratio of the enzyme, demonstrating that it can establish a maximum ΔpH of ∼3, which is insufficient to maintain the low pH observed in the vacuoles of juice sac cells in lemons and other citrus fruit. Compared with yeast and mammalian enzymes, the membrane region of the plant V-ATPase lacks subunit f and possesses an unusual configuration of transmembrane α helices. Subunit H, which inhibits ATP hydrolysis in the isolated catalytic region of V-ATPase, adopts two different conformations in the intact complex, hinting at a role in modulating activity in the intact enzyme. 履歴 登録 2022年5月3日 - ヘッダ(付随情報) 公開 2022年7月6日 - マップ公開 2022年7月6日 - 更新 2024年1月17日 - 現状 2024年1月17日 処理サイト : RCSB / 状態 : 公開
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