Skip Navigation
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

National Institute of Environmental Health Sciences

Use this QR code to view the newest version of this document
Use this QR code to view the newest version of this document

Your Environment. Your Health.

Publication Detail

Title: Stress sensor triggers conformational response of the integral membrane protein microsomal glutathione transferase 1.

Authors: Busenlehner, Laura S; Codreanu, Simona G; Holm, Peter J; Bhakat, Priyaranjan; Hebert, Hans; Morgenstern, Ralf; Armstrong, Richard N

Published In Biochemistry, (2004 Sep 07)

Abstract: Microsomal glutathione (GSH) transferase 1 (MGST1) is a trimeric, integral membrane protein involved in cellular response to chemical or oxidative stress. The cytosolic domain of MGST1 harbors the GSH binding site and a cysteine residue (C49) that acts as a sensor of oxidative and chemical stress. Spatially resolved changes in the kinetics of backbone amide H/D exchange reveal that the binding of a single molecule of GSH/trimer induces a cooperative conformational transition involving movements of the transmembrane helices and a reordering of the cytosolic domain. Alkylation of the stress sensor preorganizes the helices and facilitates the cooperative transition resulting in catalytic activation.

PubMed ID: 15366924 Exiting the NIEHS site

MeSH Terms: Amino Acid Sequence; Animals; Crystallography, X-Ray; Deuterium Exchange Measurement; Ethylmaleimide/chemistry; Glutathione Transferase/chemistry*; Glutathione Transferase/metabolism; Glutathione Transferase/ultrastructure; Glutathione/chemistry; Kinetics; Male; Mass Spectrometry; Membrane Proteins/chemistry*; Membrane Proteins/metabolism; Membrane Proteins/ultrastructure; Microsomes, Liver/enzymology*; Molecular Sequence Data; Oxidative Stress*; Peptide Fragments/chemistry; Peptide Fragments/metabolism; Protein Conformation; Proteolipids/chemistry; Proteolipids/metabolism; Rats; Rats, Sprague-Dawley

Back
to Top