EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase.
ジャーナル・号・ページ	Nature, Vol. 521, Issue 7551, Page 241-245, Year 2015
掲載日	2015年5月14日
著者	Jianhua Zhao / Samir Benlekbir / John L Rubinstein /
PubMed 要旨	Eukaryotic vacuolar H(+)-ATPases (V-ATPases) are rotary enzymes that use energy from hydrolysis of ATP to ADP to pump protons across membranes and control the pH of many intracellular compartments. ...Eukaryotic vacuolar H(+)-ATPases (V-ATPases) are rotary enzymes that use energy from hydrolysis of ATP to ADP to pump protons across membranes and control the pH of many intracellular compartments. ATP hydrolysis in the soluble catalytic region of the enzyme is coupled to proton translocation through the membrane-bound region by rotation of a central rotor subcomplex, with peripheral stalks preventing the entire membrane-bound region from turning with the rotor. The eukaryotic V-ATPase is the most complex rotary ATPase: it has three peripheral stalks, a hetero-oligomeric proton-conducting proteolipid ring, several subunits not found in other rotary ATPases, and is regulated by reversible dissociation of its catalytic and proton-conducting regions. Studies of ATP synthases, V-ATPases, and bacterial/archaeal V/A-ATPases have suggested that flexibility is necessary for the catalytic mechanism of rotary ATPases, but the structures of different rotational states have never been observed experimentally. Here we use electron cryomicroscopy to obtain structures for three rotational states of the V-ATPase from the yeast Saccharomyces cerevisiae. The resulting series of structures shows ten proteolipid subunits in the c-ring, setting the ATP:H(+) ratio for proton pumping by the V-ATPase at 3:10, and reveals long and highly tilted transmembrane α-helices in the a-subunit that interact with the c-ring. The three different maps reveal the conformational changes that occur to couple rotation in the symmetry-mismatched soluble catalytic region to the membrane-bound proton-translocating region. Almost all of the subunits of the enzyme undergo conformational changes during the transitions between these three rotational states. The structures of these states provide direct evidence that deformation during rotation enables the smooth transmission of power through rotary ATPases.
リンク	Nature / PubMed:25971514
手法	EM (単粒子)
解像度	6.9 - 8.3 Å
構造データ	6284 3j9t EMDB-6284, PDB-3j9t: Yeast V-ATPase state 1 手法: EM (単粒子) / 解像度: 6.9 Å 6285 3j9u EMDB-6285, PDB-3j9u: Yeast V-ATPase state 2 手法: EM (単粒子) / 解像度: 7.6 Å 6286 3j9v EMDB-6286, PDB-3j9v: Yeast V-ATPase state 3 手法: EM (単粒子) / 解像度: 8.3 Å
由来	saccharomyces cerevisiae (パン酵母)
キーワード	HYDROLASE / V-ATPase / V-type ATPase / vacuolar-type ATPase / proton pump