3HYP
Crystal structure of Bacteroides fragilis TrxP_S105G mutant
Summary for 3HYP
| Entry DOI | 10.2210/pdb3hyp/pdb |
| Related | 3HXS |
| Descriptor | Thioredoxin, ZINC ION (3 entities in total) |
| Functional Keywords | thioredoxin, disulfide bond, electron transport |
| Biological source | Bacteroides fragilis |
| Total number of polymer chains | 2 |
| Total formula weight | 32059.46 |
| Authors | Shouldice, S.R. (deposition date: 2009-06-22, release date: 2010-01-12, Last modification date: 2024-11-13) |
| Primary citation | Shouldice, S.R.,Cho, S.H.,Boyd, D.,Heras, B.,Eser, M.,Beckwith, J.,Riggs, P.,Martin, J.L.,Berkmen, M. In vivo oxidative protein folding can be facilitated by oxidation-reduction cycling Mol.Microbiol., 75:13-28, 2010 Cited by PubMed Abstract: Current dogma dictates that bacterial proteins with misoxidized disulfide bonds are shuffled into correctly oxidized states by DsbC. There are two proposed mechanisms for DsbC activity. The first involves a DsbC-only model of substrate disulfide rearrangement. The second invokes cycles of reduction and oxidation of substrate disulfide bonds by DsbC and DsbA respectively. Here, we addressed whether the second mechanism is important in vivo by identifying whether a periplasmic reductase could complement DsbC. We screened for naturally occurring periplasmic reductases in Bacteroides fragilis, a bacterium chosen because we predicted it encodes reductases and has a reducing periplasm. We found that the B. fragilis periplasmic protein TrxP has a thioredoxin fold with an extended N-terminal region; that it is a very active reductase but a poor isomerase; and that it fully complements dsbC. These results provide direct in vivo evidence that correctly folded protein is achievable via cycles of oxidation and reduction. PubMed: 19968787DOI: 10.1111/j.1365-2958.2009.06952.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.899 Å) |
Structure validation
Download full validation report
