1g0t
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene> | |LIGAND= <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1eej|1eej]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g0t OCA], [http://www.ebi.ac.uk/pdbsum/1g0t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g0t RCSB]</span> | ||
}} | }} | ||
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[[Category: Haebel, P W.]] | [[Category: Haebel, P W.]] | ||
[[Category: Metcalf, P.]] | [[Category: Metcalf, P.]] | ||
| - | [[Category: PEG]] | ||
[[Category: protein disulfide bond isomerase]] | [[Category: protein disulfide bond isomerase]] | ||
[[Category: thiol oxidoreductase]] | [[Category: thiol oxidoreductase]] | ||
[[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 Sun Mar 30 20:34:08 2008'' |
Revision as of 17:34, 30 March 2008
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| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Protein disulfide-isomerase, with EC number 5.3.4.1 | ||||||
| Related: | 1eej
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DSBC MUTANT C101S
Overview
DsbC is one of five Escherichia coli proteins required for disulfide bond formation and is thought to function as a disulfide bond isomerase during oxidative protein folding in the periplasm. DsbC is a 2 x 23 kDa homodimer and has both protein disulfide isomerase and chaperone activity. We report the 1.9 A resolution crystal structure of oxidized DsbC where both Cys-X-X-Cys active sites form disulfide bonds. The molecule consists of separate thioredoxin-like domains joined via hinged linker helices to an N-terminal dimerization domain. The hinges allow relative movement of the active sites, and a broad uncharged cleft between them may be involved in peptide binding and DsbC foldase activities.
About this Structure
1G0T is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli., McCarthy AA, Haebel PW, Torronen A, Rybin V, Baker EN, Metcalf P, Nat Struct Biol. 2000 Mar;7(3):196-9. PMID:10700276
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