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1k3o

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{{STRUCTURE_1k3o| PDB=1k3o | SCENE= }}
{{STRUCTURE_1k3o| PDB=1k3o | SCENE= }}
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'''Crystal Structure Analysis of apo Glutathione S-Transferase'''
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===Crystal Structure Analysis of apo Glutathione S-Transferase===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_12211029}}
==About this Structure==
==About this Structure==
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[[Category: Apo glutatione s-transferase]]
[[Category: Apo glutatione s-transferase]]
[[Category: X-ray structure]]
[[Category: X-ray structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:15:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:10:54 2008''

Revision as of 07:10, 29 July 2008

Image:1k3o.png

Template:STRUCTURE 1k3o

Crystal Structure Analysis of apo Glutathione S-Transferase

Template:ABSTRACT PUBMED 12211029

About this Structure

1K3O is a Single protein structure of sequence from Homo sapiens. 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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