1eoh
From Proteopedia
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| - | [[Image:1eoh.gif|left|200px]] | + | [[Image:1eoh.gif|left|200px]] |
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| - | '''GLUTATHIONE TRANSFERASE P1-1''' | + | {{Structure |
| + | |PDB= 1eoh |SIZE=350|CAPTION= <scene name='initialview01'>1eoh</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''GLUTATHIONE TRANSFERASE P1-1''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EOH is a [ | + | 1EOH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EOH OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10970734 10970734] |
[[Category: Glutathione transferase]] | [[Category: Glutathione transferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: helix capping mutant (d152a)]] | [[Category: helix capping mutant (d152a)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:58:19 2008'' |
Revision as of 08:58, 20 March 2008
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| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Glutathione transferase, with EC number 2.5.1.18 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Thu Mar 20 10:58:19 2008
