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

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Bibtex

@article{d2f23bead3de4f4a889a62aa18f04a5c,
title = "Stress sensor triggers conformational response of the integral membrane protein microsomal glutathione transferase 1",
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.",
author = "Busenlehner, {L S} and Codreanu, {S G} and Holm, {P J} and P Bhakat and Hans Hebert and R Morgenstern and Armstrong, {R N}",
year = "2004",
doi = "10.1021/bi048716k",
language = "English",
volume = "43",
pages = "11145--11152",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "The American Chemical Society (ACS)",
number = "35",

}