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| | ==Crystal Structure of Bacteroides fragilis TrxP== | | ==Crystal Structure of Bacteroides fragilis TrxP== |
| - | <StructureSection load='3hxs' size='340' side='right' caption='[[3hxs]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='3hxs' size='340' side='right'caption='[[3hxs]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3hxs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacteroides_inaequalis"_eggerth_and_gagnon_1933 "bacteroides inaequalis" eggerth and gagnon 1933]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HXS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HXS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3hxs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_fragilis Bacteroides fragilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HXS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HXS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.996Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">trxP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=817 "Bacteroides inaequalis" Eggerth and Gagnon 1933])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3hxs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hxs OCA], [http://pdbe.org/3hxs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hxs RCSB], [http://www.ebi.ac.uk/pdbsum/3hxs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hxs ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hxs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hxs OCA], [https://pdbe.org/3hxs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hxs RCSB], [https://www.ebi.ac.uk/pdbsum/3hxs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hxs ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q64SV7_BACFR Q64SV7_BACFR] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Thioredoxin|Thioredoxin]] | + | *[[Thioredoxin 3D structures|Thioredoxin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacteroides inaequalis eggerth and gagnon 1933]] | + | [[Category: Bacteroides fragilis]] |
| - | [[Category: Shouldice, S R]] | + | [[Category: Large Structures]] |
| - | [[Category: Electron transport]] | + | [[Category: Shouldice SR]] |
| - | [[Category: Thioredoxin]]
| + | |
| Structural highlights
Function
Q64SV7_BACFR
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Shouldice SR, Cho SH, Boyd D, Heras B, Eser M, Beckwith J, Riggs P, Martin JL, Berkmen M. In vivo oxidative protein folding can be facilitated by oxidation-reduction cycling. Mol Microbiol. 2010 Jan;75(1):13-28. Epub 2009 Dec 3. PMID:19968787 doi:10.1111/j.1365-2958.2009.06952.x
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