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

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

doi:10.1038/s42003-022-04397-3

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

Journal Article · Mon Jan 16 00:00:00 EST 2023 · Communications Biology

DOI:https://doi.org/10.1038/s42003-022-04397-3· OSTI ID:2915164

^[1]; Kang, Patrick T. ^[2]; Jiang, Ruisheng ^[3]; Lee, Jodie Y. ^[4]; Soares, Jitesh A. ^[5]; Krzycki, Joseph A. ^[6]; ^[7]

The Chinese University of Hong Kong (China)
Northeast Ohio Medical University, Rootstown, OH (United States); Ohio State University Biochemistry Program, Columbus, OH (United States)
The Ohio State University, Columbus, OH (United States)
The Ohio State University, Columbus, OH (United States); TechLab, Inc., Blacksburg, VA (United States)
The Ohio State University, Columbus, OH (United States); American Chemical Society, Washington, DC (United States)
Ohio State University Biochemistry Program, Columbus, OH (United States); The Ohio State University, Columbus, OH (United States)
The Chinese University of Hong Kong (China); Ohio State University Biochemistry Program, Columbus, OH (United States)

The 22nd genetically encoded amino acid, pyrrolysine, plays a unique role in the key step in the growth of methanogens on mono-, di-, and tri-methylamines by activating the methyl group of these substrates for transfer to a corrinoid cofactor. Previous crystal structures of the Methanosarcina barkeri monomethylamine methyltransferase elucidated the structure of pyrrolysine and provide insight into its role in monomethylamine activation. Herein, we report the second structure of a pyrrolysine-containing protein, the M. barkeri trimethylamine methyltransferase MttB, and its structure bound to sulfite, a substrate analog of trimethylamine. We also report the structure of MttB in complex with its cognate corrinoid protein MttC, which specifically receives the methyl group from the pyrrolysine-activated trimethylamine substrate during methanogenesis. Together these structures provide key insights into the role of pyrrolysine in methyl group transfer from trimethylamine to the corrinoid cofactor in MttC.

View Accepted Manuscript (DOE)

Research Organization:: The Ohio State Univ., Columbus, OH (United States); The Ohio State University, Columbus, OH (United States)

Sponsoring Organization:: National Institutes of Health (NIH); USDOE Office of Science (SC); USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences & Biosciences Division (CSGB)

Grant/Contract Number:: FG02-91ER20042

OSTI ID:: 2915164

Alternate ID(s):: OSTI ID: 2417684

Journal Information:: Communications Biology, Journal Name: Communications Biology Journal Issue: 1 Vol. 6; ISSN 2399-3642

Publisher:: Springer Science and Business Media LLCCopyright Statement

Country of Publication:: United States

Language:: English

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