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Parallel Evolutionary Pathways for Glutathione Transferases:  Structure and Mechanism of the Mitochondrial Class Kappa Enzyme rGSTK1-1†

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The Center for Advanced Research in Biotechnology of the Maryland Biotechnology Institute and the National Institutes of Standards and Technology, Gudelsky Drive, Rockville, Maryland 20850, and Departments of Biochemistry and Chemistry and Center in Molecular Toxicology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146
Cite this: Biochemistry 2004, 43, 2, 352–361
Publication Date (Web):December 19, 2003
https://doi.org/10.1021/bi035832z
Copyright © 2004 American Chemical Society
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    Abstract

    The class kappa glutathione (GSH) transferase is an enzyme that resides in the mitochondrial matrix. Its relationship to members of the canonical GSH transferase superfamily has remained an enigma. The three-dimensional structure of the class kappa enzyme from rat (rGSTK1-1) in complex with GSH has been solved by single isomorphous replacement with anomalous scattering at a resolution of 2.5 Å. The structure reveals that the enzyme is more closely related to the protein disulfide bond isomerase, dsbA, from Escherichia coli than it is to members of the canonical superfamily. The structures of rGSTK1-1 and the canonical superfamily members indicate that the proteins folds have diverged from a common thioredoxin/glutaredoxin progenitor but did so by different mechanisms. The mitochondrial enzyme, therefore, represents a fourth protein superfamily that supports GSH transferase activity. The thioredoxin domain functions in a manner that is similar to that seen in the canonical enzymes by providing key structural elements for the recognition of GSH. The hydroxyl group of S16 is within hydrogen-bonding distance of the sulfur of bound GSH and is, in part, responsible for the ionization of the thiol in the E•GSH complex (pKa = 6.4 ± 0.1). Preequilibrium kinetic experiments indicate that the kon for GSH is 1 × 105 M-1 s-1 and koff for GS- is ∼8 s-1 and relatively slow with respect to turnover with 1-chloro-2, 4-dinitrobenzene (CDNB). As a result, the KMGSH (11 mM) is much larger than the apparent KdGSH (90 μM). The active site has a relatively open access channel that is flanked by disordered loops that may explain the relatively high turnover number (280 s-1 at pH 7.0) toward CDNB. The disordered loops form an extensive contiguous patch on one face of the dimeric enzyme, a fact that suggests that the protein surface may interact with a membrane or other protein partner.

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    †

     Supported by Grants R01 GM30910, P30 ES00267, T32 ES07028, and T32 GM08320 from the National Institutes of Health. Use of the Advanced Photon Source was supported by the U.S. Department of Energy, Basic Energy Sciences, Office of Science, under Contract No. W-31-109-Eng-38. Use of the BioCARS Sector 14 was supported by the National Institutes of Health, National Center for Research Resources, under Grant No. RR07707.

    ‡

     The Center for Advanced Research in Biotechnology of the Maryland Biotechnology Institute and the National Institutes of Standards and Technology.

    §

     Vanderbilt University School of Medicine.

    *

     To whom correspondence should be addressed. Tel:  615 343-2920. Fax:  615 343-2921. E-mail:  [email protected].

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