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	Structure of the mitochondrial ATP synthase from determined by electron cryo-microscopy.
ジャーナル・号・ページ	Proc Natl Acad Sci U S A, Vol. 113, Issue 45, Page 12709-12714, Year 2016
掲載日	2016年11月8日
著者	Kutti R Vinothkumar / Martin G Montgomery / Sidong Liu / John E Walker /
PubMed 要旨	The structure of the intact monomeric ATP synthase from the fungus, , has been solved by electron cryo-microscopy. The structure provides insights into the mechanical coupling of the transmembrane ...The structure of the intact monomeric ATP synthase from the fungus, , has been solved by electron cryo-microscopy. The structure provides insights into the mechanical coupling of the transmembrane proton motive force across mitochondrial membranes in the synthesis of ATP. This mechanism requires a strong and integral stator, consisting of the catalytic αβ-domain, peripheral stalk, and, in the membrane domain, subunit a and associated supernumerary subunits, kept in contact with the rotor turning at speeds up to 350 Hz. The stator's integrity is ensured by robust attachment of both the oligomycin sensitivity conferral protein (OSCP) to the catalytic domain and the membrane domain of subunit b to subunit a. The ATP8 subunit provides an additional brace between the peripheral stalk and subunit a. At the junction between the OSCP and the apparently stiff, elongated α-helical b-subunit and associated d- and h-subunits, an elbow or joint allows the stator to bend to accommodate lateral movements during the activity of the catalytic domain. The stator may also apply lateral force to help keep the static a-subunit and rotating c-ring together. The interface between the c-ring and the a-subunit contains the transmembrane pathway for protons, and their passage across the membrane generates the turning of the rotor. The pathway has two half-channels containing conserved polar residues provided by a bundle of four α-helices inclined at ∼30° to the plane of the membrane, similar to those described in other species. The structure provides more insights into the workings of this amazing machine.
リンク	Proc Natl Acad Sci U S A / PubMed:27791192 / PubMed Central
手法	EM (単粒子)
解像度	7.0 - 7.9 Å
構造データ	4100 5lqx EMDB-4100, PDB-5lqx: Structure of F-ATPase from Pichia angusta, state3 手法: EM (単粒子) / 解像度: 7.9 Å 4101 5lqy EMDB-4101: Structure of F-ATPase from Pichia angusta, state2. PDB-5lqy: Structure of F-ATPase from Pichia angusta, in state2 手法: EM (単粒子) / 解像度: 7.8 Å 4102 5lqz EMDB-4102, PDB-5lqz: Structure of F-ATPase from Pichia angusta, state1 手法: EM (単粒子) / 解像度: 7.0 Å
化合物	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP / ATP, エネルギー貯蔵分子YM ChemComp-MG: Unknown entry / マグネシウムジカチオン ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP / ADP, エネルギー貯蔵分子YM
由来	ogataea angusta (菌類) bos taurus (ウシ)
キーワード	HYDROLASE / ATP synthase / ATP hydrolase / complex