1ZRT
Rhodobacter capsulatus cytochrome bc1 complex with stigmatellin bound
1ZRT の概要
| エントリーDOI | 10.2210/pdb1zrt/pdb |
| 関連するPDBエントリー | 1KB9 1PP9 2qjy 2yiu 6XI0 |
| 分子名称 | Cytochrome b, Cytochrome c1, Ubiquinol-cytochrome c reductase iron-sulfur subunit, ... (9 entities in total) |
| 機能のキーワード | cytochrome bc1, membrane protein, heme protein, rieske iron sulfur protein, cytochrome b, cytochrome c1, complex iii, oxidoreductase, redox enzyme, respiratory chain, stigmatellin, electron transport |
| 由来する生物種 | Rhodobacter capsulatus 詳細 |
| 細胞内の位置 | Cell membrane; Multi-pass membrane protein (Potential): D5ANZ3 Cell membrane; Single-pass membrane protein (Potential): D5ANZ4 Cell membrane; Single-pass membrane protein: D5ANZ2 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 202108.10 |
| 構造登録者 | Berry, E.A.,Huang, L.S.,Saechao, L.K.,Pon, N.G.,Valkova-Valchanov, M.,Daldal, F. (登録日: 2005-05-22, 公開日: 2005-06-07, 最終更新日: 2024-11-20) |
| 主引用文献 | Berry, E.A.,Huang, L.S.,Saechao, L.K.,Pon, N.G.,Valkova-Valchanova, M.,Daldal, F. X-Ray Structure of Rhodobacter Capsulatus Cytochrome bc (1): Comparison with its Mitochondrial and Chloroplast Counterparts. Photosynth.Res., 81:251-275, 2004 Cited by PubMed Abstract: Ubihydroquinone: cytochrome (cyt)c oxidoreductase, or cyt bc (1), is a widespread, membrane integral enzyme that plays a crucial role during photosynthesis and respiration. It is one of the major contributors of the electrochemical proton gradient, which is subsequently used for ATP synthesis. The simplest form of the cyt bc (1) is found in bacteria, and it contains only the three ubiquitously conserved catalytic subunits: the Fe-S protein, cyt b and cyt c (1). Here we present a preliminary X-ray structure of Rhodobacter capsulatus cyt bc (1) at 3.8 A and compare it to the available structures of its homologues from mitochondria and chloroplast. Using the bacterial enzyme structure, we highlight the structural similarities and differences that are found among the three catalytic subunits between the members of this family of enzymes. In addition, we discuss the locations of currently known critical mutations, and their implications in terms of the cyt bc (1) catalysis. PubMed: 16034531DOI: 10.1023/B:PRES.0000036888.18223.0e 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.51 Å) |
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