1g0t: Difference between revisions
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==DSBC MUTANT C101S== | ==DSBC MUTANT C101S== | ||
<StructureSection load='1g0t' size='340' side='right' caption='[[1g0t]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='1g0t' size='340' side='right'caption='[[1g0t]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1g0t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G0T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G0T FirstGlance]. <br> | <table><tr><td colspan='2'>[[1g0t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G0T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G0T FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1g0t" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1g0t" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Thiol:disulfide interchange protein|Thiol:disulfide interchange protein]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bacillus coli migula 1895]] | [[Category: Bacillus coli migula 1895]] | ||
[[Category: Large Structures]] | |||
[[Category: Protein disulfide-isomerase]] | [[Category: Protein disulfide-isomerase]] | ||
[[Category: Haebel, P W]] | [[Category: Haebel, P W]] | ||
Revision as of 11:23, 23 October 2019
DSBC MUTANT C101SDSBC MUTANT C101S
Structural highlights
Function[DSBC_ECOLI] Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. 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. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDsbC 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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