3hyp | pdb_00003hyp

Crystal structure of Bacteroides fragilis TrxP_S105G mutant

spinqualitylabelsall models 3hyp, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3hyp is a 2 chain structure with sequence from "bacteroides_inaequalis"_eggerth_and_gagnon_1933 "bacteroides inaequalis" eggerth and gagnon 1933. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN Related: 3hxs Gene: trxP ("Bacteroides inaequalis" Eggerth and Gagnon 1933) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. In vivo oxidative protein folding can be facilitated by oxidation-reduction cycling.,Shouldice SR, Cho SH, Boyd D, Heras B, Eser M, Beckwith J, Riggs P, Martin JL, Berkmen M Mol Microbiol. 2010 Jan;75(1):13-28. Epub 2009 Dec 3. PMID:19968787 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Thioredoxin 3D structures

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