Structural and Spectroscopic Basis for Catalysis by a Class C Radical S‑Adenosylmethionine Methylase Involved in Nosiheptide/Nocathiacin Biosynthesis
Bo Wang, Hayley L. Knox, Nicholas J. York, Matthew I. Radle, Alexey Silakov, Squire J. Booker · 2026
Read Structural and Spectroscopic Basis for Catalysis by a Class C Radical S‑Adenosylmethionine Methylase Involved in Nosiheptide/Nocathiacin Biosynthesis by Bo Wang, Hayley L. Knox, Nicholas J. York, Matthew I. Radle, Alexey Silakov, Squire J. Booker (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13266988.txt.
Description
Bo Wang and colleagues present in 2026 the first crystal structures of an enzyme family that builds part of a potent antibiotic called nosiheptide. The enzyme, studied through its relative NocN, adds a methyl group using a radical reaction that is hard to achieve in a lab. Structures were solved under oxygen-free conditions at very fine resolution.
Two bound copies of the fuel molecule SAM sit inside the enzyme, positioned so a radical can pass between them. One specific tyrosine residue emerged as central to the chemistry, and a trapped product-like molecule showed how the enzyme grips its target. Magnetic spectroscopy caught a fleeting radical species matching the proposed pathway. The pictures explain how this enzyme performs its unusual carbon chemistry.
Catalog record
| CREATOR | Bo Wang, Hayley L. Knox, Nicholas J. York, Matthew I. Radle, Alexey Silakov, Squire J. Booker |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 38 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |