A glutathione transferase from Agrobacterium tumefaciens reveals a novel class of bacterial GST superfamily.

In the present work, we report a novel class of glutathione transferases (GSTs) originated from the pathogenic soil bacterium Agrobacterium tumefaciens C58, with structural and catalytic properties not observed previously in prokaryotic and eukaryotic GST isoenzymes. A GST-like sequence from A. tume...

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Autores principales:	Katholiki Skopelitou, Prathusha Dhavala, Anastassios C Papageorgiou, Nikolaos E Labrou
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/2fd9c055d0a245769332d9d17ef57838
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spelling	oai:doaj.org-article:2fd9c055d0a245769332d9d17ef578382021-11-18T07:23:16ZA glutathione transferase from Agrobacterium tumefaciens reveals a novel class of bacterial GST superfamily.1932-620310.1371/journal.pone.0034263https://doaj.org/article/2fd9c055d0a245769332d9d17ef578382012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22496785/?tool=EBIhttps://doaj.org/toc/1932-6203In the present work, we report a novel class of glutathione transferases (GSTs) originated from the pathogenic soil bacterium Agrobacterium tumefaciens C58, with structural and catalytic properties not observed previously in prokaryotic and eukaryotic GST isoenzymes. A GST-like sequence from A. tumefaciens C58 (Atu3701) with low similarity to other characterized GST family of enzymes was identified. Phylogenetic analysis showed that it belongs to a distinct GST class not previously described and restricted only in soil bacteria, called the Eta class (H). This enzyme (designated as AtuGSTH1-1) was cloned and expressed in E. coli and its structural and catalytic properties were investigated. Functional analysis showed that AtuGSTH1-1 exhibits significant transferase activity against the common substrates aryl halides, as well as very high peroxidase activity towards organic hydroperoxides. The crystal structure of AtuGSTH1-1 was determined at 1.4 Å resolution in complex with S-(p-nitrobenzyl)-glutathione (Nb-GSH). Although AtuGSTH1-1 adopts the canonical GST fold, sequence and structural characteristics distinct from previously characterized GSTs were identified. The absence of the classic catalytic essential residues (Tyr, Ser, Cys) distinguishes AtuGSTH1-1 from all other cytosolic GSTs of known structure and function. Site-directed mutagenesis showed that instead of the classic catalytic residues, an Arg residue (Arg34), an electron-sharing network, and a bridge of a network of water molecules may form the basis of the catalytic mechanism. Comparative sequence analysis, structural information, and site-directed mutagenesis in combination with kinetic analysis showed that Phe22, Ser25, and Arg187 are additional important residues for the enzyme's catalytic efficiency and specificity.Katholiki SkopelitouPrathusha DhavalaAnastassios C PapageorgiouNikolaos E LabrouPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 4, p e34263 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Katholiki Skopelitou Prathusha Dhavala Anastassios C Papageorgiou Nikolaos E Labrou A glutathione transferase from Agrobacterium tumefaciens reveals a novel class of bacterial GST superfamily.
description	In the present work, we report a novel class of glutathione transferases (GSTs) originated from the pathogenic soil bacterium Agrobacterium tumefaciens C58, with structural and catalytic properties not observed previously in prokaryotic and eukaryotic GST isoenzymes. A GST-like sequence from A. tumefaciens C58 (Atu3701) with low similarity to other characterized GST family of enzymes was identified. Phylogenetic analysis showed that it belongs to a distinct GST class not previously described and restricted only in soil bacteria, called the Eta class (H). This enzyme (designated as AtuGSTH1-1) was cloned and expressed in E. coli and its structural and catalytic properties were investigated. Functional analysis showed that AtuGSTH1-1 exhibits significant transferase activity against the common substrates aryl halides, as well as very high peroxidase activity towards organic hydroperoxides. The crystal structure of AtuGSTH1-1 was determined at 1.4 Å resolution in complex with S-(p-nitrobenzyl)-glutathione (Nb-GSH). Although AtuGSTH1-1 adopts the canonical GST fold, sequence and structural characteristics distinct from previously characterized GSTs were identified. The absence of the classic catalytic essential residues (Tyr, Ser, Cys) distinguishes AtuGSTH1-1 from all other cytosolic GSTs of known structure and function. Site-directed mutagenesis showed that instead of the classic catalytic residues, an Arg residue (Arg34), an electron-sharing network, and a bridge of a network of water molecules may form the basis of the catalytic mechanism. Comparative sequence analysis, structural information, and site-directed mutagenesis in combination with kinetic analysis showed that Phe22, Ser25, and Arg187 are additional important residues for the enzyme's catalytic efficiency and specificity.
format	article
author	Katholiki Skopelitou Prathusha Dhavala Anastassios C Papageorgiou Nikolaos E Labrou
author_facet	Katholiki Skopelitou Prathusha Dhavala Anastassios C Papageorgiou Nikolaos E Labrou
author_sort	Katholiki Skopelitou
title	A glutathione transferase from Agrobacterium tumefaciens reveals a novel class of bacterial GST superfamily.
title_short	A glutathione transferase from Agrobacterium tumefaciens reveals a novel class of bacterial GST superfamily.
title_full	A glutathione transferase from Agrobacterium tumefaciens reveals a novel class of bacterial GST superfamily.
title_fullStr	A glutathione transferase from Agrobacterium tumefaciens reveals a novel class of bacterial GST superfamily.
title_full_unstemmed	A glutathione transferase from Agrobacterium tumefaciens reveals a novel class of bacterial GST superfamily.
title_sort	glutathione transferase from agrobacterium tumefaciens reveals a novel class of bacterial gst superfamily.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/2fd9c055d0a245769332d9d17ef57838
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A glutathione transferase from Agrobacterium tumefaciens reveals a novel class of bacterial GST superfamily.

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