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1yzx

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(New page: 200px<br /> <applet load="1yzx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yzx, resolution 1.93&Aring;" /> '''Crystal structure o...)
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Revision as of 18:21, 12 November 2007


1yzx, resolution 1.93Å

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Crystal structure of human kappa class glutathione transferase

Overview

Glutathione transferases (GSTs) are a superfamily of enzymes that play a, vital functional role in the cellular detoxification process. They, catalyze the conjugation of the thiol group of glutathione (GSH) to the, electrophilic groups of a wide range of hydrophobic substrates, leading to, an easier removal of the latter from the cells. The kappa class is the, least studied one among various classes within the superfamily. We report, here the expression, purification, and crystal structure of human kappa, class GST (hGSTK), which has been determined by the multiple-isomorphous, replacement method and refined to 1.93 A resolution. The overall structure, of hGSTK is similar to the recently reported structure of kappa class GST, from rat mitochondrion. Each subunit of the dimeric hGSTK contains a, thioredoxin (TRX)-like domain and a helical domain. A molecule of, glutathione sulfinate, an oxidized product of GSH, is found to bind at the, G site of each monomer. One oxygen atom of the sulfino group of GSF forms, a hydrogen bond with the hydroxyl group of the catalytic residue Ser16., The TRX-like domain of hGSTK shares 19% sequence identity and structure, similarity with human theta class GST, suggesting that the kappa class of, GST is more closely related to the theta class enzyme within the GST, superfamily. The structure of the TRX-like domain of hGSTK is also similar, to that of glutathione peroxidase (GPx), implying an evolutionary, relationship between GST and GPx.

About this Structure

1YZX is a Single protein structure of sequence from Homo sapiens with GSF as ligand. Active as Glutathione transferase, with EC number 2.5.1.18 Full crystallographic information is available from OCA.

Reference

Thioredoxin-like domain of human kappa class glutathione transferase reveals sequence homology and structure similarity to the theta class enzyme., Li J, Xia Z, Ding J, Protein Sci. 2005 Sep;14(9):2361-9. Epub 2005 Aug 4. PMID:16081649

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