Cargando…
Glutathione Transferases Are Structural and Functional Outliers in the Thioredoxin Fold
[Image: see text] Glutathione transferases (GSTs) are ubiquitous scavengers of toxic compounds that fall, structurally and functionally, within the thioredoxin fold suprafamily. The fundamental catalytic capability of GSTs is catalysis of the nucleophilic addition or substitution of glutathione at e...
Autores principales: | , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2009
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2778357/ https://www.ncbi.nlm.nih.gov/pubmed/19842715 http://dx.doi.org/10.1021/bi901180v |
_version_ | 1782174237369303040 |
---|---|
author | Atkinson, Holly J. Babbitt, Patricia C. |
author_facet | Atkinson, Holly J. Babbitt, Patricia C. |
author_sort | Atkinson, Holly J. |
collection | PubMed |
description | [Image: see text] Glutathione transferases (GSTs) are ubiquitous scavengers of toxic compounds that fall, structurally and functionally, within the thioredoxin fold suprafamily. The fundamental catalytic capability of GSTs is catalysis of the nucleophilic addition or substitution of glutathione at electrophilic centers in a wide range of small electrophilic compounds. While specific GSTs have been studied in detail, little else is known about the structural and functional relationships between different groupings of GSTs. Through a global analysis of sequence and structural similarity, it was determined that variation in the binding of glutathione between the two major subgroups of cytosolic (soluble) GSTs results in a different mode of glutathione activation. Additionally, the convergent features of glutathione binding between cytosolic GSTs and mitochondrial GST kappa are described. The identification of these structural and functional themes helps to illuminate some of the fundamental contributions of the thioredoxin fold to catalysis in the GSTs and clarify how the thioredoxin fold can be modified to enable new functions. |
format | Text |
id | pubmed-2778357 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | American Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-27783572009-11-17 Glutathione Transferases Are Structural and Functional Outliers in the Thioredoxin Fold Atkinson, Holly J. Babbitt, Patricia C. Biochemistry [Image: see text] Glutathione transferases (GSTs) are ubiquitous scavengers of toxic compounds that fall, structurally and functionally, within the thioredoxin fold suprafamily. The fundamental catalytic capability of GSTs is catalysis of the nucleophilic addition or substitution of glutathione at electrophilic centers in a wide range of small electrophilic compounds. While specific GSTs have been studied in detail, little else is known about the structural and functional relationships between different groupings of GSTs. Through a global analysis of sequence and structural similarity, it was determined that variation in the binding of glutathione between the two major subgroups of cytosolic (soluble) GSTs results in a different mode of glutathione activation. Additionally, the convergent features of glutathione binding between cytosolic GSTs and mitochondrial GST kappa are described. The identification of these structural and functional themes helps to illuminate some of the fundamental contributions of the thioredoxin fold to catalysis in the GSTs and clarify how the thioredoxin fold can be modified to enable new functions. American Chemical Society 2009-10-20 2009-11-24 /pmc/articles/PMC2778357/ /pubmed/19842715 http://dx.doi.org/10.1021/bi901180v Text en Copyright © 2009 American Chemical Society http://pubs.acs.org This is an open-access article distributed under the ACS AuthorChoice Terms & Conditions. Any use of this article, must conform to the terms of that license which are available at http://pubs.acs.org. |
spellingShingle | Atkinson, Holly J. Babbitt, Patricia C. Glutathione Transferases Are Structural and Functional Outliers in the Thioredoxin Fold |
title | Glutathione Transferases Are Structural and Functional Outliers in the Thioredoxin Fold |
title_full | Glutathione Transferases Are Structural and Functional Outliers in the Thioredoxin Fold |
title_fullStr | Glutathione Transferases Are Structural and Functional Outliers in the Thioredoxin Fold |
title_full_unstemmed | Glutathione Transferases Are Structural and Functional Outliers in the Thioredoxin Fold |
title_short | Glutathione Transferases Are Structural and Functional Outliers in the Thioredoxin Fold |
title_sort | glutathione transferases are structural and functional outliers in the thioredoxin fold |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2778357/ https://www.ncbi.nlm.nih.gov/pubmed/19842715 http://dx.doi.org/10.1021/bi901180v |
work_keys_str_mv | AT atkinsonhollyj glutathionetransferasesarestructuralandfunctionaloutliersinthethioredoxinfold AT babbittpatriciac glutathionetransferasesarestructuralandfunctionaloutliersinthethioredoxinfold |