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| | <StructureSection load='2iy2' size='340' side='right'caption='[[2iy2]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='2iy2' size='340' side='right'caption='[[2iy2]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2iy2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IY2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2IY2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2iy2]] is a 2 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=2IY2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IY2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</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]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1v57|1v57]], [[1v58|1v58]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></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=2iy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iy2 OCA], [http://pdbe.org/2iy2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2iy2 RCSB], [http://www.ebi.ac.uk/pdbsum/2iy2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2iy2 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=2iy2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iy2 OCA], [https://pdbe.org/2iy2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iy2 RCSB], [https://www.ebi.ac.uk/pdbsum/2iy2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iy2 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/DSBG_ECOLI DSBG_ECOLI] Involved in disulfide bond formation. 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 such as ErfK, YbiS and YnhG. Probably also functions as a disulfide isomerase with a narrower substrate specificity than DsbC. DsbG is maintained in a reduced state by DsbD. Displays chaperone activity in both redox states in vitro.<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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| | [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Metcalf, P]] | + | [[Category: Metcalf P]] |
| - | [[Category: Yeh, S M]] | + | [[Category: Yeh S-M]] |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Disulfide bond isomerase]]
| + | |
| - | [[Category: Dsbc]]
| + | |
| - | [[Category: Dsbg]]
| + | |
| - | [[Category: Periplasmic]]
| + | |
| - | [[Category: Redox-active center]]
| + | |
| Structural highlights
Function
DSBG_ECOLI Involved in disulfide bond formation. 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 such as ErfK, YbiS and YnhG. Probably also functions as a disulfide isomerase with a narrower substrate specificity than DsbC. DsbG is maintained in a reduced state by DsbD. Displays chaperone activity in both redox states in vitro.[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
DsbC and DsbG are periplasmic disulfide-bond isomerases, enzymes that facilitate the folding of secreted proteins with multiple disulfide bonds by catalyzing disulfide-bond rearrangement. Both enzymes also have in vitro chaperone activity. The crystal structures of these molecules are similar and both are V-shaped homodimeric modular structures. Each dimeric molecule contains two separate C-terminal thioredoxin-fold domains, joined by hinged helical "stalks" to a single N-terminal dimerization domain formed from the N-terminal 67 residues of each monomer. In this work, the crystal structures of the separate DsbC and DsbG dimerization domains have been determined at resolutions of 2.0 and 1.9 A, respectively. The two structures are both similar to the corresponding domains in the full-length molecules, showing that the dimerization domains fold independently of the catalytic portions of the full-length molecules. Localized structural differences between DsbC and DsbG were observed near the dimer interface and may be relevant to the different functions of the two enzymes.
Structures of the dimerization domains of the Escherichia coli disulfide-bond isomerase enzymes DsbC and DsbG.,Yeh SM, Koon N, Squire C, Metcalf P Acta Crystallogr D Biol Crystallogr. 2007 Apr;63(Pt 4):465-71. Epub 2007, Mar 16. PMID:17372350[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
- ↑ Yeh SM, Koon N, Squire C, Metcalf P. Structures of the dimerization domains of the Escherichia coli disulfide-bond isomerase enzymes DsbC and DsbG. Acta Crystallogr D Biol Crystallogr. 2007 Apr;63(Pt 4):465-71. Epub 2007, Mar 16. PMID:17372350 doi:10.1107/S0907444907003320
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