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Stress sensor triggers conformational response of the integral membrane protein microsomal glutathione transferase 1
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2004 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 43, no 35, 11145-11152 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2004. Vol. 43, no 35, 11145-11152 p.
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Biochemistry and Molecular Biology
URN: urn:nbn:se:kth:diva-82977DOI: 10.1021/bi048716kISI: 000223708400001PubMedID: 15366924OAI: diva2:498641
QC 20120224Available from: 2012-02-12 Created: 2012-02-12 Last updated: 2012-02-24Bibliographically approved

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Hebert, Hans
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