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

Busenlehner, L S ; Codreanu, S G ; Holm, P J ; Bhakat, P ; Hebert, Hans LU ; Morgenstern, R and Armstrong, R N (2004) In Biochemistry 43(35). p.11145-11152
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.
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author
; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemistry
volume
43
issue
35
pages
11145 - 11152
publisher
The American Chemical Society (ACS)
external identifiers
  • scopus:4444316044
  • pmid:15366924
ISSN
0006-2960
DOI
10.1021/bi048716k
language
English
LU publication?
yes
id
d2f23bea-d3de-4f4a-889a-62aa18f04a5c (old id 139377)
date added to LUP
2016-04-01 12:18:12
date last changed
2020-11-03 04:14:07
@article{d2f23bea-d3de-4f4a-889a-62aa18f04a5c,
  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 Bhakat, P and Hebert, Hans and Morgenstern, R and Armstrong, R N},
  issn         = {0006-2960},
  language     = {eng},
  number       = {35},
  pages        = {11145--11152},
  publisher    = {The American Chemical Society (ACS)},
  series       = {Biochemistry},
  title        = {Stress sensor triggers conformational response of the integral membrane protein microsomal glutathione transferase 1},
  url          = {http://dx.doi.org/10.1021/bi048716k},
  doi          = {10.1021/bi048716k},
  volume       = {43},
  year         = {2004},
}