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PDBsum entry 2zuq
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Oxidoreductase/immune system
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PDB id
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2zuq
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Contents |
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148 a.a.
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218 a.a.
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216 a.a.
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References listed in PDB file
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Key reference
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Title
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Dynamic nature of disulphide bond formation catalysts revealed by crystal structures of dsbb.
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Authors
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K.Inaba,
S.Murakami,
A.Nakagawa,
H.Iida,
M.Kinjo,
K.Ito,
M.Suzuki.
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Ref.
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Embo J, 2009,
28,
779-791.
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PubMed id
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Abstract
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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.
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