6NXV
Crystal structure of the theta class glutathione S-transferase from the citrus canker pathogen Xanthomonas axonopodis pv. citri, apo form
Summary for 6NXV
| Entry DOI | 10.2210/pdb6nxv/pdb |
| Related | 2C3N 4HK7 4MPG 6NV6 |
| Descriptor | Glutathione S-transferase, CHLORIDE ION, DIMETHYL SULFOXIDE, ... (4 entities in total) |
| Functional Keywords | theta class gst, glutathione s-transferase, citrus canker, plant pathogen, dehalogenase, transferase |
| Biological source | Xanthomonas axonopodis pv. citri (strain 306) |
| Total number of polymer chains | 4 |
| Total formula weight | 92567.08 |
| Authors | Hilario, E.,De Keyser, S.,Fan, L. (deposition date: 2019-02-10, release date: 2020-03-04, Last modification date: 2023-10-11) |
| Primary citation | 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 Cited by 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: 32744260DOI: 10.1107/S2059798320009274 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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