6NV6

Crystal structure of the theta class glutathione S-transferase from the citrus canker pathogen Xanthomonas axonopodis pv. citri with glutathione bound

6NV6 の概要

• エントリーDOI: 10.2210/pdb6nv6/pdb
• 関連するPDBエントリー: 2C3Q 4KH7 4MPG
• 分子名称: Glutathione S-transferase, CHLORIDE ION, GLUTATHIONE, ... (4 entities in total)
• 機能のキーワード: theta class gst, glutathione s-transferase, citrus canker, plant pathogen, dehalogenase, transferase
• 由来する生物種: Xanthomonas axonopodis pv. citri (strain 306)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 93412.74

構造登録者

Hilario, E.,De Keyser, S.,Fan, L. (登録日: 2019-02-04, 公開日: 2020-03-04, 最終更新日: 2023-10-11)

主引用文献

Hilario, E.,De Keyser, S.,Fan, L.
Structural and biochemical characterization of a glutathione transferase from the citrus canker pathogen Xanthomonas.
Acta Crystallogr D Struct Biol, 76:778-789, 2020

PubMed Abstract: The genus Xanthomonas comprises several cosmopolitan plant-pathogenic bacteria that affect more than 400 plant species, most of which are of economic interest. Citrus canker is a bacterial disease that affects citrus species, reducing fruit yield and quality, and is caused by the bacterium Xanthomonas citri subsp. citri (Xac). The Xac3819 gene, which has previously been reported to be important for citrus canker infection, encodes an uncharacterized glutathione S-transferase (GST) of 207 amino-acid residues in length (XacGST). Bacterial GSTs are implicated in a variety of metabolic processes such as protection against chemical and oxidative stresses. XacGST shares high sequence identity (45%) with the GstB dehalogenase from Escherichia coli O6:H1 strain CFT073 (EcGstB). Here, XacGST is reported to be able to conjugate glutathione (GSH) with bromoacetate with a K of 6.67 ± 0.77 mM, a k of 42.69 ± 0.32 s and a k/K of 6.40 ± 0.72 mM s under a saturated GSH concentration (3.6 mM). These values are comparable to those previously reported for EcGstB. In addition, crystal structures of XacGST were determined in the apo form (PDB entry 6nxv) and in a GSH-bound complex (PDB entry 6nv6). XacGST has a canonical GST-like fold with a conserved serine residue (Ser12) at the GSH-binding site near the N-terminus, indicating XacGST to be a serine-type GST that probably belongs to the theta-class GSTs. GSH binding stabilizes a loop of about 20 residues containing a helix that is disordered in the apo XacGST structure.

PubMed: 32744260
DOI: 10.1107/S2059798320009274

実験手法

X-RAY DIFFRACTION (2.65 Å)