3E9J
Structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB
Summary for 3E9J
| Entry DOI | 10.2210/pdb3e9j/pdb |
| Descriptor | Thiol/disulfide oxidoreductase DsbA, Thiol/disulfide oxidoreductase DsbB, UBIQUINONE-1 (3 entities in total) |
| Functional Keywords | membrane protein complex, mechanism of disulfide bond formation, oxidative protein folding in escherichia coli periplasm, x-ray crystal structure, charge transfer reaction intermediate, four helix bundle, periplasm, redox-active center, cell inner membrane, cell membrane, chaperone, electron transport, membrane, oxidoreductase, transmembrane, transport |
| Biological source | Escherichia coli K12 More |
| Cellular location | Periplasm: P0AEG4 Cell inner membrane; Multi-pass membrane protein: P0A6M2 |
| Total number of polymer chains | 4 |
| Total formula weight | 84650.35 |
| Authors | Malojcic, G.,Owen, R.L.,Glockshuber, R. (deposition date: 2008-08-22, release date: 2008-11-25, Last modification date: 2024-10-30) |
| Primary citation | Malojcic, G.,Owen, R.L.,Grimshaw, J.P.,Glockshuber, R. Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB. Febs Lett., 582:3301-3307, 2008 Cited by PubMed Abstract: Disulfide bond formation is a critical step in the folding of many secretory proteins. In bacteria, disulfide bonds are introduced by the periplasmic dithiol oxidase DsbA, which transfers its catalytic disulfide bond to folding polypeptides. Reduced DsbA is reoxidized by ubiquinone Q8, catalyzed by inner membrane quinone reductase DsbB. Here, we report the preparation of a kinetically stable ternary complex between wild-type DsbB, containing all essential cysteines, Q8 and DsbA covalently bound to DsbB. The crystal structure of this trapped DsbB reaction intermediate exhibits a charge-transfer interaction between Q8 and the Cys44 in the DsbB reaction center providing experimental evidence for the mechanism of de novo disulfide bond generation in DsbB. PubMed: 18775700DOI: 10.1016/j.febslet.2008.07.063 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.7 Å) |
Structure validation
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