1v57
From Proteopedia
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|PDB= 1v57 |SIZE=350|CAPTION= <scene name='initialview01'>1v57</scene>, resolution 2.Å | |PDB= 1v57 |SIZE=350|CAPTION= <scene name='initialview01'>1v57</scene>, resolution 2.Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= dsbG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= dsbG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1v58|1V58]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v57 OCA], [http://www.ebi.ac.uk/pdbsum/1v57 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1v57 RCSB]</span> | ||
}} | }} | ||
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[[Category: Raina, S.]] | [[Category: Raina, S.]] | ||
[[Category: Schirra, H J.]] | [[Category: Schirra, H J.]] | ||
| - | [[Category: SO4]] | ||
[[Category: oxidized dsbg]] | [[Category: oxidized dsbg]] | ||
[[Category: protein disulfide isomerase]] | [[Category: protein disulfide isomerase]] | ||
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[[Category: thioredoxin fold]] | [[Category: thioredoxin fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:19:35 2008'' |
Revision as of 21:19, 30 March 2008
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| , resolution 2.Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | dsbG (Escherichia coli) | ||||||
| Related: | 1V58
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the Disulfide Bond Isomerase DsbG
Overview
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.
About this Structure
1V57 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from 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:15184683
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