Stress sensor triggers conformational response of the integral membrane protein microsomal glutathione transferase 1
(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.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/139377
- author
- Busenlehner, L S ; Codreanu, S G ; Holm, P J ; Bhakat, P ; Hebert, Hans LU ; Morgenstern, R and Armstrong, R N
- organization
- publishing date
- 2004
- 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
- 2022-02-18 20:44:14
@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}}, }