2ZUP

Updated crystal structure of DsbB-DsbA complex from E. coli

2ZUP の概要

• エントリーDOI: 10.2210/pdb2zup/pdb
• 関連するPDBエントリー: 2HI7 2ZUQ
• 分子名称: Thiol:disulfide interchange protein dsbA, Disulfide bond formation protein B, ZINC ION, ... (4 entities in total)
• 機能のキーワード: disulfide bond, membrane protein, e. coli, periplasm, redox-active center, cell inner membrane, cell membrane, chaperone, electron transport, membrane, oxidoreductase, transmembrane, transport
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Periplasm: P0AEG4; Cell inner membrane ; Multi- pass membrane protein : P0A6M2
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41545.64

構造登録者

Inaba, K.,Suzuki, M.,Murakami, S.,Nakagawa, A. (登録日: 2008-10-28, 公開日: 2009-04-14, 最終更新日: 2024-11-13)

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

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: 19214188
DOI: 10.1038/emboj.2009.21

実験手法

X-RAY DIFFRACTION (3.7 Å)