1eog: Difference between revisions

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[[Image:1eog.gif|left|200px]]
{{Seed}}
[[Image:1eog.png|left|200px]]


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{{STRUCTURE_1eog|  PDB=1eog  |  SCENE=  }}  
{{STRUCTURE_1eog|  PDB=1eog  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF PI CLASS GLUTATHIONE TRANSFERASE'''
===CRYSTAL STRUCTURE OF PI CLASS GLUTATHIONE TRANSFERASE===




==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
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{{ABSTRACT_PUBMED_10970734}}


==About this Structure==
==About this Structure==
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[[Category: Stenberg, G.]]
[[Category: Stenberg, G.]]
[[Category: Glutathione transferase]]
[[Category: Glutathione transferase]]
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