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2K74

Solution NMR structure of DsbB-ubiquinone complex

Summary for 2K74
Entry DOI10.2210/pdb2k74/pdb
Related2HI7 2K73
DescriptorDisulfide bond formation protein B, UBIQUINONE-2 (2 entities in total)
Functional Keywordsmembrane protein, disulfide bond, redox enzyme, dsbb, ubiquinone, oxidative protein folding, chaperone, electron transport, inner membrane, oxidoreductase, redox-active center, transmembrane, transport
Biological sourceEscherichia coli
Cellular locationCell inner membrane; Multi-pass membrane protein: P0A6M2
Total number of polymer chains1
Total formula weight21267.20
Authors
Zhou, Y.,Cierpicki, T.,Flores Jimenez, R.H.,Lukasik, S.M.,Ellena, J.F.,Cafiso, D.S.,Kadokura, H.,Beckwith, J.,Bushweller, J.H. (deposition date: 2008-08-01, release date: 2008-10-07, Last modification date: 2021-10-20)
Primary citationZhou, Y.,Cierpicki, T.,Jimenez, R.H.,Lukasik, S.M.,Ellena, J.F.,Cafiso, D.S.,Kadokura, H.,Beckwith, J.,Bushweller, J.H.
NMR solution structure of the integral membrane enzyme DsbB: functional insights into DsbB-catalyzed disulfide bond formation.
Mol.Cell, 31:896-908, 2008
Cited by
PubMed Abstract: We describe the NMR structure of DsbB, a polytopic helical membrane protein. DsbB, a bacterial cytoplasmic membrane protein, plays a key role in disulfide bond formation. It reoxidizes DsbA, the periplasmic protein disulfide oxidant, using the oxidizing power of membrane-embedded quinones. We determined the structure of an interloop disulfide bond form of DsbB, an intermediate in catalysis. Analysis of the structure and interactions with substrates DsbA and quinone reveals functionally relevant changes induced by these substrates. Analysis of the structure, dynamics measurements, and NMR chemical shifts around the interloop disulfide bond suggest how electron movement from DsbA to quinone through DsbB is regulated and facilitated. Our results demonstrate the extraordinary utility of NMR for functional characterization of polytopic integral membrane proteins and provide insights into the mechanism of DsbB catalysis.
PubMed: 18922471
DOI: 10.1016/j.molcel.2008.08.028
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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