1ac1: Difference between revisions

Revision as of 16:33, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ac1.png

Template:STRUCTURE 1ac1

DSBA MUTANT H32LDSBA MUTANT H32L

Template:ABSTRACT PUBMED 9300489

About this StructureAbout this Structure

1AC1 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability., Guddat LW, Bardwell JC, Glockshuber R, Huber-Wunderlich M, Zander T, Martin JL, Protein Sci. 1997 Sep;6(9):1893-900. PMID:9300489

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''DSBA MUTANT H32L'''
+===DSBA MUTANT H32L===
-==Overview==
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-DsbA, a 21-kDa protein from Escherichia coli, is a potent oxidizing disulfide catalyst required for disulfide bond formation in secreted proteins. The active site of DsbA is similar to that of mammalian protein disulfide isomerases, and includes a reversible disulfide bond formed from cysteines separated by two residues (Cys30-Pro31-His32-Cys33). Unlike most protein disulfides, the active-site disulfide of DsbA is highly reactive and the oxidized form of DsbA is much less stable than the reduced form at physiological pH. His32, one of the two residues between the active-site cysteines, is critical to the oxidizing power of DsbA and to the relative instability of the protein in the oxidized form. Mutation of this single residue to tyrosine, serine, or leucine results in a significant increase in stability (of approximately 5-7 kcal/mol) of the oxidized His32 variants relative to the oxidized wild-type protein. Despite the dramatic changes in stability, the structures of all three oxidized DsbA His32 variants are very similar to the wild-type oxidized structure, including conservation of solvent atoms near the active-site residue, Cys30. These results show that the His32 residue does not exert a conformational effect on the structure of DsbA. The destabilizing effect of His32 on oxidized DsbA is therefore most likely electrostatic in nature.
+The line below this paragraph, {{ABSTRACT_PUBMED_9300489}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9300489 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_9300489}}
 ==About this Structure==
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 [[Category: Redox-active center]]
 [[Category: Thioredoxin fold]]
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