Crystal structures of human MGST2 reveal synchronized conformational changes regulating catalysis

Madhuranayaki Thulasingam; Laura Orellana; Emmanuel Nji; Shabbir Ahmad; Agnes Rinaldo-Matthis; Jesper Z. Haeggström

doi:10.1038/s41467-021-21924-8

Nature Communications (Mar 2021)

Crystal structures of human MGST2 reveal synchronized conformational changes regulating catalysis

Madhuranayaki Thulasingam,
Laura Orellana,
Emmanuel Nji,
Shabbir Ahmad,
Agnes Rinaldo-Matthis,
Jesper Z. Haeggström

Affiliations

Madhuranayaki Thulasingam: Department of Medical Biochemistry and Biophysics, Division of Chemistry II, Karolinska Institutet
Laura Orellana: Department of Biochemistry and Biophysics, Stockholm University
Emmanuel Nji: Department of Biochemistry and Biophysics, Stockholm University
Shabbir Ahmad: Department of Medical Biochemistry and Biophysics, Division of Chemistry II, Karolinska Institutet
Agnes Rinaldo-Matthis: Department of Medical Biochemistry and Biophysics, Division of Chemistry II, Karolinska Institutet
Jesper Z. Haeggström: Department of Medical Biochemistry and Biophysics, Division of Chemistry II, Karolinska Institutet

DOI: https://doi.org/10.1038/s41467-021-21924-8
Journal volume & issue: Vol. 12, no. 1
pp. 1 – 12

Abstract

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Microsomal glutathione S-transferase 2 (MGST2) produces leukotriene C4, an intracrine mediator of cell death. Structural, biochemical and computational analyses of human MGST2 suggest a mechanism employed by the enzyme to restrict catalysis to only one active site within the MGST2 trimer.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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