1k3o
From Proteopedia
(New page: 200px<br /> <applet load="1k3o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k3o, resolution 1.8Å" /> '''Crystal Structure An...) |
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| - | [[Image:1k3o. | + | [[Image:1k3o.jpg|left|200px]]<br /><applet load="1k3o" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1k3o, resolution 1.8Å" /> | caption="1k3o, resolution 1.8Å" /> | ||
'''Crystal Structure Analysis of apo Glutathione S-Transferase'''<br /> | '''Crystal Structure Analysis of apo Glutathione S-Transferase'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1K3O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Full crystallographic information is available from [http:// | + | 1K3O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K3O OCA]. |
==Reference== | ==Reference== | ||
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[[Category: x-ray structure]] | [[Category: x-ray structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:11:16 2008'' |
Revision as of 14:11, 15 February 2008
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Crystal Structure Analysis of apo Glutathione S-Transferase
Overview
Cytosolic glutathione S-transferases (GSTs) play a critical role in, xenobiotic binding and metabolism, as well as in modulation of oxidative, stress. Here, the high-resolution X-ray crystal structures of homodimeric, human GSTA1-1 in the apo form and in complex with S-hexyl glutathione (two, data sets) are reported at 1.8, 1.5, and 1.3A respectively. At this level, of resolution, distinct conformations of the alkyl chain of S-hexyl, glutathione are observed, reflecting the nonspecific nature of the, hydrophobic substrate binding site (H-site). Also, an extensive network of, ordered water, including 75 discrete solvent molecules, traverses the open, subunit-subunit interface and connects the glutathione binding sites in, each subunit. In the highest-resolution structure, three glycerol moieties, lie within this network and directly connect the amino termini of the, glutathione molecules. A search for ligand binding sites with the docking, program Molecular Operating Environment identified the ordered water, network binding site, lined mainly with hydrophobic residues, suggesting, an extended ligand binding surface for nonsubstrate ligands, the so-called, ligandin site. Finally, detailed comparison of the structures reported, here with previously published X-ray structures reveal a possible reaction, coordinate for ligand-dependent conformational changes in the active site, and the C-terminus.
About this Structure
1K3O 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
1.3-A resolution structure of human glutathione S-transferase with S-hexyl glutathione bound reveals possible extended ligandin binding site., Le Trong I, Stenkamp RE, Ibarra C, Atkins WM, Adman ET, Proteins. 2002 Sep 1;48(4):618-27. PMID:12211029
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