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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: No MeSH terms associated with this publication

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