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| {{STRUCTURE_1eog| PDB=1eog | SCENE= }} | | {{STRUCTURE_1eog| PDB=1eog | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF PI CLASS GLUTATHIONE TRANSFERASE'''
| | ===CRYSTAL STRUCTURE OF PI CLASS GLUTATHIONE TRANSFERASE=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_10970734}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10970734 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10970734}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Stenberg, G.]] | | [[Category: Stenberg, G.]] |
| [[Category: Glutathione transferase]] | | [[Category: Glutathione transferase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:20:39 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 01:18:30 2008'' |