2YCD

Structure of a novel Glutathione Transferase from Agrobacterium tumefaciens.

2YCD の概要

• エントリーDOI: 10.2210/pdb2ycd/pdb
• 分子名称: GLUTATHIONE S-TRANSFERASE, S-(P-NITROBENZYL)GLUTATHIONE, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: transferase, soil bacteria, herbicide detoxification
• 由来する生物種: AGROBACTERIUM TUMEFACIENS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26710.36

構造登録者

Skopelitou, K.,Dhavala, P.,Papageorgiou, A.C.,Labrou, N.E. (登録日: 2011-03-13, 公開日: 2012-03-28, 最終更新日: 2024-05-08)

主引用文献

Skopelitou, K.,Dhavala, P.,Papageorgiou, A.C.,Labrou, N.E.
A Glutathione Transferase from Agrobacterium Tumefaciens Reveals a Novel Class of Bacterial Gst Superfamily.
Plos One, 7:34263-, 2012

PubMed Abstract: 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.

PubMed: 22496785
DOI: 10.1371/JOURNAL.PONE.0034263

実験手法

X-RAY DIFFRACTION (1.4 Å)