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1ydk
From Proteopedia
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| - | [[Image:1ydk.gif|left|200px]] | + | [[Image:1ydk.gif|left|200px]] |
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| - | '''Crystal structure of the I219A mutant of human glutathione transferase A1-1 with S-hexylglutathione''' | + | {{Structure |
| + | |PDB= 1ydk |SIZE=350|CAPTION= <scene name='initialview01'>1ydk</scene>, resolution 1.950Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=GTX:S-HEXYLGLUTATHIONE'>GTX</scene> | ||
| + | |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= GSTA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the I219A mutant of human glutathione transferase A1-1 with S-hexylglutathione''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YDK is a [ | + | 1YDK 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=1YDK OCA]. |
==Reference== | ==Reference== | ||
| - | Tertiary interactions stabilise the C-terminal region of human glutathione transferase A1-1: a crystallographic and calorimetric study., Kuhnert DC, Sayed Y, Mosebi S, Sayed M, Sewell T, Dirr HW, J Mol Biol. 2005 Jun 17;349(4):825-38. PMID:[http:// | + | Tertiary interactions stabilise the C-terminal region of human glutathione transferase A1-1: a crystallographic and calorimetric study., Kuhnert DC, Sayed Y, Mosebi S, Sayed M, Sewell T, Dirr HW, J Mol Biol. 2005 Jun 17;349(4):825-38. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15893769 15893769] |
[[Category: Glutathione transferase]] | [[Category: Glutathione transferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: s-hexylglutathione]] | [[Category: s-hexylglutathione]] | ||
| - | ''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 15:21:32 2008'' |
Revision as of 13:21, 20 March 2008
| |||||||
| , resolution 1.950Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | GSTA1 (Homo sapiens) | ||||||
| Activity: | Glutathione transferase, with EC number 2.5.1.18 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the I219A mutant of human glutathione transferase A1-1 with S-hexylglutathione
Overview
The C-terminal region in class Alpha glutathione transferase A1-1 (GSTA1-1), which forms an amphipathic alpha-helix (helix 9), is known to contribute to the catalytic and non-substrate ligand-binding functions of the enzyme. The region in the apo protein is proposed to be disordered which, upon ligand binding at the active-site, becomes structured and localised. Because Ile219 plays a pivotal role in the stability and localisation of the region, the role of tertiary interactions mediated by Ile219 in determining the conformation and dynamics of the C-terminal region were studied. Ligand-binding microcalorimetric and X-ray structural data were obtained to characterise ligand binding at the active-site and the associated localisation of the C-terminal region. In the crystal structure of the I219A hGSTA1-1.S-hexylglutathione complex, the C-terminal region of one chain is mobile and not observed (unresolved electron density), whereas the corresponding region of the other chain is localised and structured as a result of crystal packing interactions. In solution, the mutant C-terminal region of both chains in the complex is mobile and delocalised resulting in a hydrated, less hydrophobic active-site and a reduction in the affinity of the protein for S-hexylglutathione. Complete dehydration of the active-site, important for maintaining the highly reactive thiolate form of glutathione, requires the binding of ligands and the subsequent localisation of the C-terminal region. Thermodynamic data demonstrate that the mobile C-terminal region in apo hGSTA1-1 is structured and does not undergo ligand-induced folding. Its close proximity to the surface of the wild-type protein is indicated by the concurrence between the observed heat capacity change of complex formation and the type and amount of surface area that becomes buried at the ligand-protein interface when the C-terminal region in the apo protein assumes the same localised structure as that observed in the wild-type complex.
About this Structure
1YDK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Tertiary interactions stabilise the C-terminal region of human glutathione transferase A1-1: a crystallographic and calorimetric study., Kuhnert DC, Sayed Y, Mosebi S, Sayed M, Sewell T, Dirr HW, J Mol Biol. 2005 Jun 17;349(4):825-38. PMID:15893769
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