A YafK family protein from Legionella pneumophila exhibits serine-dependent β-lactam hydrolysis activity
Wenwen Xu, Yuan Cao, Liangsan Cao, Changyong Xiao, Wenjie Sun, Zhenhuang Ge, Weiqiang Wang, Jiajia Gao, Honghua Ge · 2026
Read A YafK family protein from Legionella pneumophila exhibits serine-dependent β-lactam hydrolysis activity by Wenwen Xu, Yuan Cao, Liangsan Cao, Changyong Xiao, Wenjie Sun, Zhenhuang Ge, Weiqiang Wang, Jiajia Gao, Honghua Ge (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/PMC13400389.txt.
Description
Wenwen Xu and co-authors characterize, in 2026, a bacterial protein named Lpg1514 from Legionella pneumophila, the germ behind Legionnaires disease. The protein belongs to a family thought to cut amide bonds using a cysteine residue. Whether the same scaffold could support other chemistry was unknown.
Crystal views showed the expected fold and a clear pocket for its target. Tests then found the protein could break down beta-lactam antibiotics, a major drug class, but the work depended on a serine residue, not the usual cysteine. Mutant studies backed that unusual route. In living bacteria the protein aided drug tolerance only modestly, hinting at brief contact with antibiotics rather than strong destruction.
Catalog record
| CREATOR | Wenwen Xu, Yuan Cao, Liangsan Cao, Changyong Xiao, Wenjie Sun, Zhenhuang Ge, Weiqiang Wang, Jiajia Gao, Honghua Ge |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 29233 |
| LICENSE | https://creativecommons.org/licenses/by/4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |