Insights into pyrrolysine function from structures of a trimethylamine methyltransferase and its corrinoid protein complex
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.
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2023-01-01
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| Series: | Communications Biology |
| Online Access: | https://doi.org/10.1038/s42003-022-04397-3 |
| _version_ | 1797945752231608320 |
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| author | Jiaxin Li Patrick T. Kang Ruisheng Jiang Jodie Y. Lee Jitesh A. Soares Joseph A. Krzycki Michael K. Chan |
| author_facet | Jiaxin Li Patrick T. Kang Ruisheng Jiang Jodie Y. Lee Jitesh A. Soares Joseph A. Krzycki Michael K. Chan |
| author_sort | Jiaxin Li |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-10T21:00:06Z |
| format | Article |
| id | doaj.art-951eef061d2a4d528aa1b7b838c12b17 |
| institution | Directory Open Access Journal |
| issn | 2399-3642 |
| language | English |
| last_indexed | 2024-04-10T21:00:06Z |
| publishDate | 2023-01-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Communications Biology |
| spelling | doaj.art-951eef061d2a4d528aa1b7b838c12b172023-01-22T12:22:19ZengNature PortfolioCommunications Biology2399-36422023-01-016111010.1038/s42003-022-04397-3Insights into pyrrolysine function from structures of a trimethylamine methyltransferase and its corrinoid protein complexJiaxin Li0Patrick T. Kang1Ruisheng Jiang2Jodie Y. Lee3Jitesh A. Soares4Joseph A. Krzycki5Michael K. Chan6School of Life Sciences, and Center of Novel Biomaterials, The Chinese University of Hong Kong, ShatinDepartment of Integrative Medical Sciences, College of Medicine, Northeast Ohio Medical UniversityDepartment of Microbiology, The Ohio State UniversityDepartment of Microbiology, The Ohio State UniversityDepartment of Microbiology, The Ohio State UniversityOhio State University Biochemistry ProgramSchool of Life Sciences, and Center of Novel Biomaterials, The Chinese University of Hong Kong, ShatinStructures 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.https://doi.org/10.1038/s42003-022-04397-3 |
| spellingShingle | Jiaxin Li Patrick T. Kang Ruisheng Jiang Jodie Y. Lee Jitesh A. Soares Joseph A. Krzycki Michael K. Chan Insights into pyrrolysine function from structures of a trimethylamine methyltransferase and its corrinoid protein complex Communications Biology |
| title | Insights into pyrrolysine function from structures of a trimethylamine methyltransferase and its corrinoid protein complex |
| title_full | Insights into pyrrolysine function from structures of a trimethylamine methyltransferase and its corrinoid protein complex |
| title_fullStr | Insights into pyrrolysine function from structures of a trimethylamine methyltransferase and its corrinoid protein complex |
| title_full_unstemmed | Insights into pyrrolysine function from structures of a trimethylamine methyltransferase and its corrinoid protein complex |
| title_short | Insights into pyrrolysine function from structures of a trimethylamine methyltransferase and its corrinoid protein complex |
| title_sort | insights into pyrrolysine function from structures of a trimethylamine methyltransferase and its corrinoid protein complex |
| url | https://doi.org/10.1038/s42003-022-04397-3 |
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