2K74
Solution NMR structure of DsbB-ubiquinone complex
Summary for 2K74
| Entry DOI | 10.2210/pdb2k74/pdb |
| Related | 2HI7 2K73 |
| Descriptor | Disulfide bond formation protein B, UBIQUINONE-2 (2 entities in total) |
| Functional Keywords | membrane protein, disulfide bond, redox enzyme, dsbb, ubiquinone, oxidative protein folding, chaperone, electron transport, inner membrane, oxidoreductase, redox-active center, transmembrane, transport |
| Biological source | Escherichia coli |
| Cellular location | Cell inner membrane; Multi-pass membrane protein: P0A6M2 |
| Total number of polymer chains | 1 |
| Total formula weight | 21267.20 |
| 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 citation | Zhou, 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: 18922471DOI: 10.1016/j.molcel.2008.08.028 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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