2iyj: Difference between revisions
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|PDB= 2iyj |SIZE=350|CAPTION= <scene name='initialview01'>2iyj</scene>, resolution 2.00Å | |PDB= 2iyj |SIZE=350|CAPTION= <scene name='initialview01'>2iyj</scene>, resolution 2.00Å | ||
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+B'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iyj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iyj OCA], [http://www.ebi.ac.uk/pdbsum/2iyj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2iyj RCSB]</span> | |||
}} | }} | ||
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[[Category: Metcalf, P.]] | [[Category: Metcalf, P.]] | ||
[[Category: Yeh, S-.M.]] | [[Category: Yeh, S-.M.]] | ||
[[Category: disulfide bond isomerase]] | [[Category: disulfide bond isomerase]] | ||
[[Category: dsbc]] | [[Category: dsbc]] | ||
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[[Category: redox-active center]] | [[Category: redox-active center]] | ||
''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 03:50:29 2008'' | ||
Revision as of 03:50, 31 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE N-TERMINAL DIMER DOMAIN OF E.COLI DSBC
OverviewOverview
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.
About this StructureAbout this Structure
2IYJ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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
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