2CLY

Subcomplex of the stator of bovine mitochondrial ATP synthase

2CLY の概要

• エントリーDOI: 10.2210/pdb2cly/pdb
• 関連するPDBエントリー: 1VZS
• 分子名称: ATP SYNTHASE B CHAIN, MITOCHONDRIAL, ATP SYNTHASE D CHAIN, MITOCHONDRIAL, ATP SYNTHASE COUPLING FACTOR 6, MITOCHONDRIAL, ... (4 entities in total)
• 機能のキーワード: mitochondria, mitochondrion, ion transport, cf(0), stator, transport, acetylation, atp synthase, hydrogen ion transport, transit peptide, peripheral stalk, hydrolase
• 由来する生物種: BOS TAURUS (BOVINE); 詳細
• 細胞内の位置: Mitochondrion: P13619 P13620 P02721
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 104818.44

構造登録者

Kane Dickson, V.,Silvester, J.A.,Fearnley, I.M.,Leslie, A.G.W.,Walker, J.E. (登録日: 2006-05-03, 公開日: 2006-06-28, 最終更新日: 2024-05-08)

主引用文献

Kane Dickson, V.,Silvester, J.A.,Fearnley, I.M.,Leslie, A.G.W.,Walker, J.E.
On the Structure of the Stator of the Mitochondrial ATP Synthase.
Embo J., 25:2911-, 2006

PubMed Abstract: The structure of most of the peripheral stalk, or stator, of the F-ATPase from bovine mitochondria, determined at 2.8 A resolution, contains residues 79-183, 3-123 and 5-70 of subunits b, d and F6, respectively. It consists of a continuous curved alpha-helix about 160 A long in the single b-subunit, augmented by the predominantly alpha-helical d- and F6-subunits. The structure occupies most of the peripheral stalk in a low-resolution structure of the F-ATPase. The long helix in subunit b extends from near to the top of the F1 domain to the surface of the membrane domain, and it probably continues unbroken across the membrane. Its uppermost region interacts with the oligomycin sensitivity conferral protein, bound to the N-terminal region of one alpha-subunit in the F1 domain. Various features suggest that the peripheral stalk is probably rigid rather than resembling a flexible rope. It remains unclear whether the transient storage of energy required by the rotary mechanism takes place in the central stalk or in the peripheral stalk or in both domains.

PubMed: 16791136
DOI: 10.1038/SJ.EMBOJ.7601177

実験手法

X-RAY DIFFRACTION (2.8 Å)