PDBsum entry 6f05

Transferase

PDB id: 6f05

Contents

Protein chains

(+ 3 more) 204 a.a.

193 a.a.

Ligands

GTS ×10

GOL ×4

Metals

_CL ×9

Waters ×735

PDB id:

6f05

Name:

Transferase

Title:

Arabidopsis thaliana gstf9, gso3 bound

Structure:

Glutathione s-transferase f9. Chain: a, b, c, d, e, f, g, h, i, j. Synonym: atgstf9,atgstf7,gst class-phi member 9. Engineered: yes

Source:

Arabidopsis thaliana. Mouse-ear cress. Organism_taxid: 3702. Gene: gstf9, gluttr, gstf7, at2g30860, f7f1.7. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.20Å R-factor: 0.164 R-free: 0.209

Authors:

M.A.Tossounian,K.Wahni,I.Vanmolle,D.Vertommen,L.Rosado,J.Messens

Key ref:

M.A.Tossounian et al. (2019). Redox-regulated methionine oxidation of Arabidopsis thaliana glutathione transferase Phi9 induces H-site flexibility. Protein Sci, 28, 56-67. PubMed id: 29732642 DOI: 10.1002/pro.3440

Date:

17-Nov-17 Release date: 15-Aug-18

Protein chains

O80852  (GSTF9_ARATH) -  Glutathione S-transferase F9 from Arabidopsis thaliana

Seq: 215 a.a.

Struc: 204 a.a.

Protein chain

O80852  (GSTF9_ARATH) -  Glutathione S-transferase F9 from Arabidopsis thaliana

Seq: 215 a.a.

Struc: 193 a.a.

Enzyme reactions

• Enzyme class: Chains A, B, C, D, E, F, G, H, I, J: E.C.2.5.1.18 - glutathione transferase.
• Reaction: RX + glutathione = an S-substituted glutathione + a halide anion + H⁺

RX (Bound ligand (Het Group name = GTS) matches with 86.96% similarity) + glutathione = S-substituted glutathione + halide anion + H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1002/pro.3440

Protein Sci 28:56-67 (2019)

PubMed id: 29732642

Redox-regulated methionine oxidation of Arabidopsis thaliana glutathione transferase Phi9 induces H-site flexibility.

M.A.Tossounian, K.Wahni, I.Van Molle, D.Vertommen, L.Astolfi Rosado, J.Messens.

ABSTRACT

Glutathione transferase enzymes help plants to cope with biotic and abiotic stress. They mainly catalyze the conjugation of glutathione (GSH) onto xenobiotics, and some act as glutathione peroxidase. With X-ray crystallography, kinetics, and thermodynamics, we studied the impact of oxidation on Arabidopsis thaliana glutathione transferase Phi 9 (GSTF9). GSTF9 has no cysteine in its sequence, and it adopts a universal GST structural fold characterized by a typical conserved GSH-binding site (G-site) and a hydrophobic co-substrate-binding site (H-site). At elevated H₂ O₂ concentrations, methionine sulfur oxidation decreases its transferase activity. This oxidation increases the flexibility of the H-site loop, which is reflected in lower activities for hydrophobic substrates. Determination of the transition state thermodynamic parameters shows that upon oxidation an increased enthalpic penalty is counterbalanced by a more favorable entropic contribution. All in all, to guarantee functionality under oxidative stress conditions, GSTF9 employs a thermodynamic and structural compensatory mechanism and becomes substrate of methionine sulfoxide reductases, making it a redox-regulated enzyme.