Insights into pyrrolysine function from structures of a trimethylamine methyltransferase and its corrinoid protein complex

Jiaxin Li; Patrick T. Kang; Ruisheng Jiang; Jodie Y. Lee; Jitesh A. Soares; Joseph A. Krzycki; Michael K. Chan

doi:10.1038/s42003-022-04397-3

Communications Biology (Jan 2023)

Insights into pyrrolysine function from structures of a trimethylamine methyltransferase and its corrinoid protein complex

Jiaxin Li,
Patrick T. Kang,
Ruisheng Jiang,
Jodie Y. Lee,
Jitesh A. Soares,
Joseph A. Krzycki,
Michael K. Chan

Affiliations

Jiaxin Li: School of Life Sciences, and Center of Novel Biomaterials, The Chinese University of Hong Kong, Shatin
Patrick T. Kang: Department of Integrative Medical Sciences, College of Medicine, Northeast Ohio Medical University
Ruisheng Jiang: Department of Microbiology, The Ohio State University
Jodie Y. Lee: Department of Microbiology, The Ohio State University
Jitesh A. Soares: Department of Microbiology, The Ohio State University
Joseph A. Krzycki: Ohio State University Biochemistry Program
Michael K. Chan: School of Life Sciences, and Center of Novel Biomaterials, The Chinese University of Hong Kong, Shatin

DOI: https://doi.org/10.1038/s42003-022-04397-3
Journal volume & issue: Vol. 6, no. 1
pp. 1 – 10

Abstract

Read online

Structures of Methanosarcina barkeri trimethylamine methyltransferase (MttB) with its substrates reveal the role of pyrrolysine in methyl group transfer from trimethylamine to the corrinoid cofactor in MttC.

Published in Communications Biology

ISSN: 2399-3642 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science: Biology (General)
Website: https://www.nature.com/commsbio/

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