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| | <StructureSection load='1tjd' size='340' side='right'caption='[[1tjd]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='1tjd' size='340' side='right'caption='[[1tjd]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1tjd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TJD OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1TJD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1tjd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TJD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TJD FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DSBC, XPRA, B2893, Z4231, ECS3765 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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]] 2.5Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] </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=1tjd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tjd OCA], [https://pdbe.org/1tjd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tjd RCSB], [https://www.ebi.ac.uk/pdbsum/1tjd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tjd ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1tjd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tjd OCA], [http://pdbe.org/1tjd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1tjd RCSB], [http://www.ebi.ac.uk/pdbsum/1tjd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1tjd ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DSBC_ECOLI DSBC_ECOLI]] Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD.<ref>PMID:19965429</ref> | + | [https://www.uniprot.org/uniprot/DSBC_ECOLI DSBC_ECOLI] Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD.<ref>PMID:19965429</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Protein disulfide-isomerase]]
| + | [[Category: Banaszak K]] |
| - | [[Category: Banaszak, K]] | + | [[Category: Frost G]] |
| - | [[Category: Frost, G]] | + | [[Category: Mechin I]] |
| - | [[Category: Mechin, I]] | + | [[Category: Rypniewski W]] |
| - | [[Category: Rypniewski, W]] | + | |
| - | [[Category: Dimer]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| Structural highlights
Function
DSBC_ECOLI Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD.[1]
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
Disufide-bond isomerase (DsbC) plays a crucial role in folding periplasmically excreted bacterial proteins. The crystal structure of the reduced form of DsbC is presented. The pair of thiol groups from Cys98 and Cys101 that form the reversible disulfide bond in the enzymatic active site are 3.1 A apart and the electron density clearly shows that the S atoms do not form a covalent bond. The other pair of Cys residues (141 and 163) in DsbC form a disulfide bond. This is different from the previously reported crystal form of DsbC (McCarthy et al., 2000), in which both Cys pairs are oxidized. Specific hydrogen-bond interactions are identified that stabilize the active site in the reactive reduced state with the special participation of hydrogen bonds between the active-site cysteine residues (98 and 101) and threonine residues 94 and 182. The present structure also differs in the orientation of the catalytic domains within the protein dimer. This is evidence of flexibility within the protein that probably plays a role in accommodating the substrates in the cleft between the catalytic domains.
Structure of the reduced disulfide-bond isomerase DsbC from Escherichia coli.,Banaszak K, Mechin I, Frost G, Rypniewski W Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1747-52. Epub 2004, Sep 23. PMID:15388920[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Depuydt M, Leonard SE, Vertommen D, Denoncin K, Morsomme P, Wahni K, Messens J, Carroll KS, Collet JF. A periplasmic reducing system protects single cysteine residues from oxidation. Science. 2009 Nov 20;326(5956):1109-11. doi: 10.1126/science.1179557. PMID:19965429 doi:http://dx.doi.org/10.1126/science.1179557
- ↑ Banaszak K, Mechin I, Frost G, Rypniewski W. Structure of the reduced disulfide-bond isomerase DsbC from Escherichia coli. Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1747-52. Epub 2004, Sep 23. PMID:15388920 doi:10.1107/S0907444904018359
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