1ep8
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ep7|1EP7]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ep8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ep8 OCA], [http://www.ebi.ac.uk/pdbsum/1ep8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ep8 RCSB]</span> | ||
}} | }} | ||
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[[Category: mutant]] | [[Category: mutant]] | ||
| - | ''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 20:07:08 2008'' |
Revision as of 17:07, 30 March 2008
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| , resolution 2.20Å | |||||||
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| Related: | 1EP7
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
About this Structure
1EP8 is a Single protein structure of sequence from Chlamydomonas reinhardtii. Full crystallographic information is available from OCA.
Reference
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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