PDBsum entry 5g5e

Transferase

PDB id: 5g5e

Contents

Protein chain

220 a.a.

Ligands

ACT

PEG ×3

Waters ×408

PDB id:

5g5e

Name:

Transferase

Title:

Crystallographic structure of the tau class glutathione s-transferase migstu from mango mangifera indica l.

Structure:

Tau class glutathione s-transferase. Chain: a. Engineered: yes

Source:

Mangifera indica. Common mango variety haden. Organism_taxid: 29780. Expressed in: escherichia coli. Expression_system_taxid: 469008. Other_details: the migstu sequence was identified from a mango haden mesocarp cdna shotgun-cdna sequencing project.

Resolution:

1.80Å R-factor: 0.163 R-free: 0.190

Authors:

I.Valenzuela-Chavira,H.Serrano-Posada,A.Lopez-Zavala,J.Hernandez- Paredes,R.Sotelo-Mundo

Key ref:

I.Valenzuela-Chavira et al. (2017). Insights into ligand binding to a glutathione S-transferase from mango: Structure, thermodynamics and kinetics. Biochimie, 135, 35-45. PubMed id: 28104507

Date:

24-May-16 Release date: 01-Feb-17

Protein chain

A0A1P8NWC2  (A0A1P8NWC2_MANIN) -  glutathione transferase from Mangifera indica

Seq: 229 a.a.

Struc: 220 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⁺

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

Added reference

Biochimie 135:35-45 (2017)

PubMed id: 28104507

Insights into ligand binding to a glutathione S-transferase from mango: Structure, thermodynamics and kinetics.

I.Valenzuela-Chavira, C.A.Contreras-Vergara, A.A.Arvizu-Flores, H.Serrano-Posada, A.A.Lopez-Zavala, K.D.García-Orozco, J.Hernandez-Paredes, E.Rudiño-Piñera, V.Stojanoff, R.R.Sotelo-Mundo, M.A.Islas-Osuna.

ABSTRACT

We studied a mango glutathione S-transferase (GST) (Mangifera indica) bound to glutathione (GSH) and S-hexyl glutathione (GSX). This GST Tau class (MiGSTU) had a molecular mass of 25.5 kDa. MiGSTU Michaelis-Menten kinetic constants were determined for their substrates obtaining a Km, Vmax and kcat for CDNB of 0.792 mM, 80.58 mM min(-1) and 68.49 s(-1) respectively and 0.693 mM, 105.32 mM min(-1) and 89.57 s(-1), for reduced GSH respectively. MiGSTU had a micromolar affinity towards GSH (5.2 μM) or GSX (7.8 μM). The crystal structure of the MiGSTU in apo or bound to GSH or GSX generated a model that explains the thermodynamic signatures of binding and showed the importance of enthalpic-entropic compensation in ligand binding to Tau-class GST enzymes.