5KEJ

Crystallographic structure of the Tau class glutathione S-transferase MiGSTU in complex with S-hexyl-glutathione

Summary for 5KEJ

• Entry DOI: 10.2210/pdb5kej/pdb
• Descriptor: Tau class glutathione S-transferase, S-HEXYLGLUTATHIONE, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• Functional Keywords: detoxification, transferase
• Biological source: Mangifera indica
• Total number of polymer chains: 2
• Total formula weight: 52523.07

Authors

Valenzuela-Chavira, I.,Serrano-Posada, H.,Lopez-Zavala, A.,Hernandez-Paredes, J.,Sotelo-Mundo, R. (deposition date: 2016-06-09, release date: 2017-02-01, Last modification date: 2023-09-27)

Primary citation

Valenzuela-Chavira, I.,Contreras-Vergara, C.A.,Arvizu-Flores, A.A.,Serrano-Posada, H.,Lopez-Zavala, A.A.,Garcia-Orozco, K.D.,Hernandez-Paredes, J.,Rudino-Pinera, E.,Stojanoff, V.,Sotelo-Mundo, R.R.,Islas-Osuna, M.A.
Insights into ligand binding to a glutathione S-transferase from mango: Structure, thermodynamics and kinetics.
Biochimie, 135:35-45, 2017

PubMed 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 K, V and k for CDNB of 0.792 mM, 80.58 mM min and 68.49 s respectively and 0.693 mM, 105.32 mM min and 89.57 s, 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.

PubMed: 28104507
DOI: 10.1016/j.biochi.2017.01.005

Experimental method

X-RAY DIFFRACTION (2.35 Å)