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1v57

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(New page: 200px<br /><applet load="1v57" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v57, resolution 2.&Aring;" /> '''Crystal Structure of t...)
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[[Image:1v57.gif|left|200px]]<br /><applet load="1v57" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1v57, resolution 2.&Aring;" />
 
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'''Crystal Structure of the Disulfide Bond Isomerase DsbG'''<br />
 
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==Overview==
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==Crystal Structure of the Disulfide Bond Isomerase DsbG==
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Dsb proteins control the formation and rearrangement of disulfide bonds, during the folding of secreted and membrane proteins in bacteria. DsbG, a, member of this family, has disulfide bond isomerase and chaperone, activity. Here, we present two crystal structures of DsbG at 1.7and 2.0-A, resolution that are meant to represent the reduced and oxidized forms, respectively. The oxidized structure, however, reveals a mixture of both, redox forms, suggesting that oxidized DsbG is less stable than the reduced, form. This trait would contribute to DsbG isomerase activity, which, requires that the active-site Cys residues are kept reduced, regardless of, the highly oxidative environment of the periplasm. We propose that a Thr, residue that is conserved in the cis-Pro loop of DsbG and DsbC but not, found in other Dsb proteins could play a role in this process. Also, the, structure of DsbG reveals an unanticipated and surprising feature that may, help define its specific role in oxidative protein folding. Thus, the, dimensions and surface features of DsbG show a very large and charged, binding surface that is consistent with interaction with globular protein, substrates having charged surfaces. This finding suggests that, rather, than catalyzing disulfide rearrangement in unfolded substrates, DsbG may, preferentially act later in the folding process to catalyze disulfide, rearrangement in folded or partially folded proteins.
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<StructureSection load='1v57' size='340' side='right'caption='[[1v57]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1v57]] 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=1V57 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V57 FirstGlance]. <br>
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</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&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1v57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v57 OCA], [https://pdbe.org/1v57 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v57 RCSB], [https://www.ebi.ac.uk/pdbsum/1v57 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v57 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v5/1v57_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1v57 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1V57 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V57 OCA].
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*[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]]
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== References ==
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==Reference==
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<references/>
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Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide., Heras B, Edeling MA, Schirra HJ, Raina S, Martin JL, Proc Natl Acad Sci U S A. 2004 Jun 15;101(24):8876-81. Epub 2004 Jun 7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15184683 15184683]
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Edeling, M.A.]]
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[[Category: Edeling MA]]
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[[Category: Heras, B.]]
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[[Category: Heras B]]
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[[Category: Martin, J.L.]]
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[[Category: Martin JL]]
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[[Category: Raina, S.]]
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[[Category: Raina S]]
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[[Category: Schirra, H.J.]]
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[[Category: Schirra HJ]]
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[[Category: SO4]]
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[[Category: oxidized dsbg]]
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[[Category: protein disulfide isomerase]]
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[[Category: redox protein]]
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[[Category: strained redox-active center]]
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[[Category: thioredoxin fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:26:39 2007''
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Current revision

Crystal Structure of the Disulfide Bond Isomerase DsbG

PDB ID 1v57

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