PDBsum entry 3fhs

Transferase

PDB id: 3fhs

Contents

Protein chains

216 a.a. *

Ligands

GSH ×2

Waters ×100

* Residue conservation analysis

Obsolete entry

PDB id:

3fhs

Name:

Transferase

Title:

Glutathione transferase from glycine max at 2.7 resolution

Structure:

2,4-d inducible glutathione s-transferase. Chain: a, b. Engineered: yes

Source:

Glycine max. Soybean. Organism_taxid: 3847. Gene: gst 4(gmgst4-4), gsta. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.71Å R-factor: 0.192 R-free: 0.241

Authors:

I.Axarli,D.Prathusha,A.C.Papageorgiou,N.E.Labrou

Key ref:

I.Axarli et al. (2009). Crystal structure of Glycine max glutathione transferase in complex with glutathione: investigation of the mechanism operating by the Tau class glutathione transferases. Biochem J, 422, 247-256. PubMed id: 19538182

Date:

10-Dec-08 Release date: 07-Jul-09

Protein chains

O49235  (O49235_SOYBN) -  Glutathione S-transferase from Glycine max

Seq: 219 a.a.

Struc: 216 a.a.

Enzyme reactions

• Enzyme class: E.C.2.5.1.18 - glutathione transferase.
• Reaction: RX + glutathione = an S-substituted glutathione + a halide anion + H⁺

RX + glutathione (Bound ligand (Het Group name = GSH) corresponds exactly) = S-substituted glutathione + halide anion + H(+)

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

Added reference

Biochem J 422:247-256 (2009)

PubMed id: 19538182

Crystal structure of Glycine max glutathione transferase in complex with glutathione: investigation of the mechanism operating by the Tau class glutathione transferases.

I.Axarli, P.Dhavala, A.C.Papageorgiou, N.E.Labrou.

ABSTRACT

Cytosolic GSTs (glutathione transferases) are a multifunctional group of enzymes widely distributed in Nature and involved in cellular detoxification processes. The three-dimensional structure of GmGSTU4-4 (Glycine max GST Tau 4-4) complexed with GSH was determined by the molecular replacement method at 2.7 A (1 A=0.1 nm) resolution. The bound GSH is located in a region formed by the beginning of alpha-helices H1, H2 and H3 in the N-terminal domain of the enzyme. Significant differences in the G-site (GSH-binding site) as compared with the structure determined in complex with Nb-GSH [S-(p-nitrobenzyl)-glutathione] were found. These differences were identified in the hydrogen-bonding and electrostatic interaction pattern and, consequently, GSH was found bound in two different conformations. In one subunit, the enzyme forms a complex with the ionized form of GSH, whereas in the other subunit it can form a complex with the non-ionized form. However, only the ionized form of GSH may form a productive and catalytically competent complex. Furthermore, a comparison of the GSH-bound structure with the Nb-GSH-bound structure shows a significant movement of the upper part of alpha-helix H4 and the C-terminal. This indicates an intrasubunit modulation between the G-site and the H-site (electrophile-binding site), suggesting that the enzyme recognizes the xenobiotic substrates by an induced-fit mechanism. The reorganization of Arg111 and Tyr107 upon xenobiotic substrate binding appears to govern the intrasubunit structural communication between the G- and H-site and the binding of GSH. The structural observations were further verified by steady-state kinetic analysis and site-directed mutagenesis studies.