1g0t

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[[Image:1g0t.jpg|left|200px]]
[[Image:1g0t.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1g0t |SIZE=350|CAPTION= <scene name='initialview01'>1g0t</scene>, resolution 2.60&Aring;
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The line below this paragraph, containing "STRUCTURE_1g0t", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1g0t| PDB=1g0t | SCENE= }}
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|RELATEDENTRY=[[1eej|1eej]]
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|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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}}
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'''DSBC MUTANT C101S'''
'''DSBC MUTANT C101S'''
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[[Category: Haebel, P W.]]
[[Category: Haebel, P W.]]
[[Category: Metcalf, P.]]
[[Category: Metcalf, P.]]
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[[Category: protein disulfide bond isomerase]]
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[[Category: Protein disulfide bond isomerase]]
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[[Category: thiol oxidoreductase]]
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[[Category: Thiol oxidoreductase]]
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[[Category: thioredoxin fold]]
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[[Category: Thioredoxin fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:59:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:34:08 2008''
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Revision as of 13:59, 2 May 2008

Image:1g0t.jpg

Template:STRUCTURE 1g0t

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 Page seeded by OCA on Fri May 2 16:59:22 2008

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