1eoh
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(New page: 200px<br /> <applet load="1eoh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eoh, resolution 2.5Å" /> '''GLUTATHIONE TRANSFER...)
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Revision as of 14:38, 12 November 2007
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GLUTATHIONE TRANSFERASE P1-1
Overview
An N-capping box motif (Ser/Thr-Xaa-Xaa-Asp) is strictly conserved at the, beginning of helix alpha6 in the core of virtually all glutathione, transferases (GST) and GST-related proteins. It has been demonstrated that, this local motif is important in determining the alpha-helical propensity, of the isolated alpha6-peptide and plays a crucial role in the folding and, stability of GSTs. Its removal by site-directed mutagenesis generated, temperature-sensitive folding mutants unable to refold at physiological, temperature (37 degrees C). In the present work, variants of human GSTP1-1, (S150A and D153A), in which the capping residues have been substituted by, alanine, have been generated and purified for structural analysis. Thus, for the first time, temperature-sensitive folding mutants of an enzyme, expressed at a permissive temperature, have been crystallized and their, three-dimensional structures determined by X-ray crystallography. The, crystal structures of human pi class GST temperature-sensitive mutants, provide a basis for understanding the structural origin of the dramatic, effects observed on the overall stability of the enzyme at higher, temperatures upon single substitution of a capping residue.
About this Structure
1EOH is a Single protein structure of sequence from Homo sapiens. Active as Glutathione transferase, with EC number 2.5.1.18 Full crystallographic information is available from OCA.
Reference
Structures of thermolabile mutants of human glutathione transferase P1-1., Rossjohn J, McKinstry WJ, Oakley AJ, Parker MW, Stenberg G, Mannervik B, Dragani B, Cocco R, Aceto A, J Mol Biol. 2000 Sep 15;302(2):295-302. PMID:10970734
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