2ZUQ
Crystal structure of DsbB-Fab complex
2ZUQ の概要
| エントリーDOI | 10.2210/pdb2zuq/pdb |
| 関連するPDBエントリー | 2HI7 2ZUP |
| 分子名称 | Disulfide bond formation protein B, Fab fragment light chain, Fab fragment heavy chain, ... (4 entities in total) |
| 機能のキーワード | disulfide bond, membrane protein, fab, e. coli, cell inner membrane, cell membrane, chaperone, electron transport, membrane, oxidoreductase, redox-active center, transmembrane, transport, oxidoreductase-immune system complex, oxidoreductase/immune system |
| 由来する生物種 | Escherichia coli 詳細 |
| 細胞内の位置 | Cell inner membrane; Multi-pass membrane protein: P0A6M2 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 140776.27 |
| 構造登録者 | |
| 主引用文献 | Inaba, K.,Murakami, S.,Nakagawa, A.,Iida, H.,Kinjo, M.,Ito, K.,Suzuki, M. Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of DsbB Embo J., 28:779-791, 2009 Cited by PubMed Abstract: In the Escherichia coli system catalysing oxidative protein folding, disulphide bonds are generated by the cooperation of DsbB and ubiquinone and transferred to substrate proteins through DsbA. The structures solved so far for different forms of DsbB lack the Cys104-Cys130 initial-state disulphide that is directly donated to DsbA. Here, we report the 3.4 A crystal structure of a DsbB-Fab complex, in which DsbB has this principal disulphide. Its comparison with the updated structure of the DsbB-DsbA complex as well as with the recently reported NMR structure of a DsbB variant having the rearranged Cys41-Cys130 disulphide illuminated conformational transitions of DsbB induced by the binding and release of DsbA. Mutational studies revealed that the membrane-parallel short alpha-helix of DsbB has a key function in physiological electron flow, presumably by controlling the positioning of the Cys130-containing loop. These findings demonstrate that DsbB has developed the elaborate conformational dynamism to oxidize DsbA for continuous protein disulphide bond formation in the cell. PubMed: 19214188DOI: 10.1038/emboj.2009.21 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.3 Å) |
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