1GMJ
The structure of bovine IF1, the regulatory subunit of mitochondrial F-ATPase
1GMJ の概要
| エントリーDOI | 10.2210/pdb1gmj/pdb |
| 関連するPDBエントリー | 1HF9 |
| 分子名称 | ATPASE INHIBITOR (1 entity in total) |
| 機能のキーワード | atpase inhibitor, bovine f1-atpase inhibitor protein, coiled-coil structure, p dependent oligomerization, atp hydrolysis |
| 由来する生物種 | BOS TAURUS (BOVINE) |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 38382.29 |
| 構造登録者 | Cabezon, E.,Runswick, M.J.,Leslie, A.G.W.,Walker, J.E. (登録日: 2001-09-14, 公開日: 2002-01-01, 最終更新日: 2024-05-08) |
| 主引用文献 | Cabezon, E.,Runswick, M.J.,Leslie, A.G.W.,Walker, J.E. The Structure of Bovine If(1), the Regulatory Subunit of Mitochondrial F-ATPase. Embo J., 20:6990-, 2001 Cited by PubMed Abstract: In mitochondria, the hydrolytic activity of ATP synthase is regulated by an inhibitor protein, IF(1). Its binding to ATP synthase depends on pH, and below neutrality, IF(1) is dimeric and forms a stable complex with the enzyme. At higher pH values, IF(1) forms tetramers and is inactive. In the 2.2 A structure of the bovine IF(1) described here, the four monomers in the asymmetric unit are arranged as a dimer of dimers. Monomers form dimers via an antiparallel alpha-helical coiled coil in the C-terminal region. Dimers are associated into oligomers and form long fibres in the crystal lattice, via coiled-coil interactions in the N-terminal and inhibitory regions (residues 14-47). Therefore, tetramer formation masks the inhibitory region, preventing IF(1) binding to ATP synthase. PubMed: 11742976DOI: 10.1093/EMBOJ/20.24.6990 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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