2ZUQ

Crystal structure of DsbB-Fab complex

Summary for 2ZUQ

• Entry DOI: 10.2210/pdb2zuq/pdb
• Related: 2HI7 2ZUP
• Descriptor: Disulfide bond formation protein B, Fab fragment light chain, Fab fragment heavy chain, ... (4 entities in total)
• Functional Keywords: 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
• Biological source: Escherichia coli; More
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P0A6M2
• Total number of polymer chains: 6
• Total formula weight: 140776.27

Authors

Inaba, K.,Suzuki, M.,Murakami, S. (deposition date: 2008-10-28, release date: 2009-04-14, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.3 Å)