Identification, characterization, and crystal structure of the omega class glutathione transferases

P. G. Board; M. Coggan; G. Chelvanayagam; S. Easteal; L. S. Jermiin; G. K. Schulte; D. E. Danley; L. R. Hoth; M. C. Griffor; A. V. Kamath; M. H. Rosner; B. A. Chrunyk; D. E. Perregaux; C. A. Gabel; K. F. Geoghegan; J. Pandit

doi:10.1074/jbc.M001706200

Identification, characterization, and crystal structure of the omega class glutathione transferases

P. G. Board, M. Coggan, G. Chelvanayagam, S. Easteal, L. S. Jermiin, G. K. Schulte, D. E. Danley, L. R. Hoth, M. C. Griffor, A. V. Kamath, M. H. Rosner, B. A. Chrunyk, D. E. Perregaux, C. A. Gabel, K. F. Geoghegan, J. Pandit

The John Curtin School of Medical Research

Research output: Contribution to a Journal (Peer & Non Peer) › Article › peer-review

637 Citations (Scopus)

Abstract

A new class of glutathione transferases has been discovered by analysis of the expressed sequence tag data base and sequence alignment. Glutathione S-transferases (GSTs) of the new class, named Omega, exist in several mammalian species and Caenorhabditis elegans. In humans, GSTO 1-1 is expressed in most tissues and exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities characteristic of the glutaredoxins. The structure of GSTO 1-1 has been determined at 2.0-Å resolution and has a characteristic GST fold (Protein Data Bank entry code leem). The Omega class GSTs exhibit an unusual N-terminal extension that abuts the C terminus to form a novel structural unit, Unlike other mammalian GSTs, GSTO 1-1 appears to have an active site cysteine that can form a disulfide bond with glutathione.

Original language	English
Pages (from-to)	24798-24806
Number of pages	9
Journal	Journal of Biological Chemistry
Volume	275
Issue number	32
DOIs	https://doi.org/10.1074/jbc.M001706200
Publication status	Published - 11 Aug 2000
Externally published	Yes

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Board, P. G., Coggan, M., Chelvanayagam, G., Easteal, S., Jermiin, L. S., Schulte, G. K., Danley, D. E., Hoth, L. R., Griffor, M. C., Kamath, A. V., Rosner, M. H., Chrunyk, B. A., Perregaux, D. E., Gabel, C. A., Geoghegan, K. F., & Pandit, J. (2000). Identification, characterization, and crystal structure of the omega class glutathione transferases. Journal of Biological Chemistry, 275(32), 24798-24806. https://doi.org/10.1074/jbc.M001706200

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title = "Identification, characterization, and crystal structure of the omega class glutathione transferases",

abstract = "A new class of glutathione transferases has been discovered by analysis of the expressed sequence tag data base and sequence alignment. Glutathione S-transferases (GSTs) of the new class, named Omega, exist in several mammalian species and Caenorhabditis elegans. In humans, GSTO 1-1 is expressed in most tissues and exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities characteristic of the glutaredoxins. The structure of GSTO 1-1 has been determined at 2.0-{\AA} resolution and has a characteristic GST fold (Protein Data Bank entry code leem). The Omega class GSTs exhibit an unusual N-terminal extension that abuts the C terminus to form a novel structural unit, Unlike other mammalian GSTs, GSTO 1-1 appears to have an active site cysteine that can form a disulfide bond with glutathione.",

author = "Board, \{P. G.\} and M. Coggan and G. Chelvanayagam and S. Easteal and Jermiin, \{L. S.\} and Schulte, \{G. K.\} and Danley, \{D. E.\} and Hoth, \{L. R.\} and Griffor, \{M. C.\} and Kamath, \{A. V.\} and Rosner, \{M. H.\} and Chrunyk, \{B. A.\} and Perregaux, \{D. E.\} and Gabel, \{C. A.\} and Geoghegan, \{K. F.\} and J. Pandit",

year = "2000",

month = aug,

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doi = "10.1074/jbc.M001706200",

language = "English",

volume = "275",

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journal = "Journal of Biological Chemistry",

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publisher = "American Society for Biochemistry and Molecular Biology Inc.",

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Board, PG, Coggan, M, Chelvanayagam, G, Easteal, S, Jermiin, LS, Schulte, GK, Danley, DE, Hoth, LR, Griffor, MC, Kamath, AV, Rosner, MH, Chrunyk, BA, Perregaux, DE, Gabel, CA, Geoghegan, KF & Pandit, J 2000, 'Identification, characterization, and crystal structure of the omega class glutathione transferases', Journal of Biological Chemistry, vol. 275, no. 32, pp. 24798-24806. https://doi.org/10.1074/jbc.M001706200

TY - JOUR

T1 - Identification, characterization, and crystal structure of the omega class glutathione transferases

AU - Board, P. G.

AU - Coggan, M.

AU - Chelvanayagam, G.

AU - Easteal, S.

AU - Jermiin, L. S.

AU - Schulte, G. K.

AU - Danley, D. E.

AU - Hoth, L. R.

AU - Griffor, M. C.

AU - Kamath, A. V.

AU - Rosner, M. H.

AU - Chrunyk, B. A.

AU - Perregaux, D. E.

AU - Gabel, C. A.

AU - Geoghegan, K. F.

AU - Pandit, J.

PY - 2000/8/11

Y1 - 2000/8/11

N2 - A new class of glutathione transferases has been discovered by analysis of the expressed sequence tag data base and sequence alignment. Glutathione S-transferases (GSTs) of the new class, named Omega, exist in several mammalian species and Caenorhabditis elegans. In humans, GSTO 1-1 is expressed in most tissues and exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities characteristic of the glutaredoxins. The structure of GSTO 1-1 has been determined at 2.0-Å resolution and has a characteristic GST fold (Protein Data Bank entry code leem). The Omega class GSTs exhibit an unusual N-terminal extension that abuts the C terminus to form a novel structural unit, Unlike other mammalian GSTs, GSTO 1-1 appears to have an active site cysteine that can form a disulfide bond with glutathione.

AB - A new class of glutathione transferases has been discovered by analysis of the expressed sequence tag data base and sequence alignment. Glutathione S-transferases (GSTs) of the new class, named Omega, exist in several mammalian species and Caenorhabditis elegans. In humans, GSTO 1-1 is expressed in most tissues and exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities characteristic of the glutaredoxins. The structure of GSTO 1-1 has been determined at 2.0-Å resolution and has a characteristic GST fold (Protein Data Bank entry code leem). The Omega class GSTs exhibit an unusual N-terminal extension that abuts the C terminus to form a novel structural unit, Unlike other mammalian GSTs, GSTO 1-1 appears to have an active site cysteine that can form a disulfide bond with glutathione.

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DO - 10.1074/jbc.M001706200

M3 - Article

SN - 0021-9258

VL - 275

SP - 24798

EP - 24806

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 32

ER -

Identification, characterization, and crystal structure of the omega class glutathione transferases

Abstract

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