1ep8: Difference between revisions

Revision as of 01:28, 1 July 2008

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File:1ep8.png

Template:STRUCTURE 1ep8

CRYSTAL STRUCTURE OF A MUTATED THIOREDOXIN, D30A, FROM CHLAMYDOMONAS REINHARDTIICRYSTAL STRUCTURE OF A MUTATED THIOREDOXIN, D30A, FROM CHLAMYDOMONAS REINHARDTII

Template:ABSTRACT PUBMED 11563970

About this StructureAbout this Structure

1EP8 is a Single protein structure of sequence from Chlamydomonas reinhardtii. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism., Menchise V, Corbier C, Didierjean C, Saviano M, Benedetti E, Jacquot JP, Aubry A, Biochem J. 2001 Oct 1;359(Pt 1):65-75. PMID:11563970

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OCA

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-[[Image:1ep8.gif|left|200px]]
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-'''CRYSTAL STRUCTURE OF A MUTATED THIOREDOXIN, D30A, FROM CHLAMYDOMONAS REINHARDTII'''
+===CRYSTAL STRUCTURE OF A MUTATED THIOREDOXIN, D30A, FROM CHLAMYDOMONAS REINHARDTII===
-==Overview==
+<!--
-Thioredoxins are ubiquitous proteins which catalyse the reduction of disulphide bridges on target proteins. The catalytic mechanism proceeds via a mixed disulphide intermediate whose breakdown should be enhanced by the involvement of a conserved buried residue, Asp-30, as a base catalyst towards residue Cys-39. We report here the crystal structure of wild-type and D30A mutant thioredoxin h from Chlamydomonas reinhardtii, which constitutes the first crystal structure of a cytosolic thioredoxin isolated from a eukaryotic plant organism. The role of residue Asp-30 in catalysis has been revisited since the distance between the carboxylate OD1 of Asp-30 and the sulphur SG of Cys-39 is too great to support the hypothesis of direct proton transfer. A careful analysis of all available crystal structures reveals that the relative positioning of residues Asp-30 and Cys-39 as well as hydrophobic contacts in the vicinity of residue Asp-30 do not allow a conformational change sufficient to bring the two residues close enough for a direct proton transfer. This suggests that protonation/deprotonation of Cys-39 should be mediated by a water molecule. Molecular-dynamics simulations, carried out either in vacuo or in water, as well as proton-inventory experiments, support this hypothesis. The results are discussed with respect to biochemical and structural data.
+The line below this paragraph, {{ABSTRACT_PUBMED_11563970}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11563970 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11563970}}
 ==About this Structure==
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 [[Category: Electron transport]]
 [[Category: Mutant]]
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