1v57: Difference between revisions

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[[Image:1v57.png|left|200px]]


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==Crystal Structure of the Disulfide Bond Isomerase DsbG==
The line below this paragraph, containing "STRUCTURE_1v57", creates the "Structure Box" on the page.
<StructureSection load='1v57' size='340' side='right'caption='[[1v57]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
{{STRUCTURE_1v57| PDB=1v57 |  SCENE= }}
<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>
</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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v5/1v57_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>


===Crystal Structure of the Disulfide Bond Isomerase DsbG===
==See Also==
 
*[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]]
 
== References ==
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{{ABSTRACT_PUBMED_15184683}}
 
==About this Structure==
1V57 is a [[Single protein]] structure of 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=1V57 OCA].
 
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/15184683 15184683]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Edeling, M A.]]
[[Category: Edeling MA]]
[[Category: Heras, B.]]
[[Category: Heras B]]
[[Category: Martin, J L.]]
[[Category: Martin JL]]
[[Category: Raina, S.]]
[[Category: Raina S]]
[[Category: Schirra, H J.]]
[[Category: Schirra HJ]]
[[Category: Oxidized dsbg]]
[[Category: Protein disulfide isomerase]]
[[Category: Redox protein]]
[[Category: Strained redox-active center]]
[[Category: Thioredoxin fold]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:29:24 2008''

Latest revision as of 09:17, 3 April 2024

Crystal Structure of the Disulfide Bond Isomerase DsbGCrystal Structure of the Disulfide Bond Isomerase DsbG

Structural highlights

1v57 is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

See Also

References

  1. ↑ 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

1v57, resolution 2.00Å

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