Structural insight into the distinct regulatory mechanism of the HEPN–MNT toxin-antitoxin system in Legionella pneumophila
Chenglong Jin, Cha-Hee Jeon, Heung Wan Kim, Jin Mo Kang, Yuri Choi, Sung-Min Kang, Hyung Ho Lee, Do-Hee Kim, Byung Woo Han, Bong-Jin Lee · 2024
Read Structural insight into the distinct regulatory mechanism of the HEPN–MNT toxin-antitoxin system in Legionella pneumophila by Chenglong Jin, Cha-Hee Jeon, Heung Wan Kim, Jin Mo Kang, Yuri Choi, Sung-Min Kang, Hyung Ho Lee, Do-Hee Kim, Byung Woo Han, Bong-Jin Lee (2024) 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-11586414.txt.
Description
Chenglong Jin and co-authors reveal, in a 2024 study, how a bacterial toxin and its antidote protein control each other in the germ that causes Legionnaires' disease. Many bacteria carry toxin-antitoxin pairs, where the antidote keeps a harmful protein in check. In this pair, the antitoxin is an enzyme that tags the toxin with a small chemical piece, switching it off. The team solved the three-dimensional shapes of the toxin, the antitoxin, and the two joined together.
Their structures show the toxin is an enzyme that cuts RNA and needs a metal ion to work, and they pinpoint its active site. The antitoxin in this species lacks a tail found in relatives, so it grips the toxin in a distinct way. From these details the authors lay out a full picture of how the pair is regulated, adding to knowledge of this toxin family.
Catalog record
| CREATOR | Chenglong Jin, Cha-Hee Jeon, Heung Wan Kim, Jin Mo Kang, Yuri Choi, Sung-Min Kang, Hyung Ho Lee, Do-Hee Kim, Byung Woo Han, Bong-Jin Lee |
|---|---|
| YEAR | 2024 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 68 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |