Structural Analysis of the Putative Succinyl-Diaminopimelic Acid Desuccinylase DapE from Campylobacter jejuni: Captopril-Mediated Structural Stabilization
Si Yeon Ahn, Young-Bong You, Han Byeol Oh, Min-Ah Park, Sung-il Yoon, Guangfeng Zhou · 2025
Read Structural Analysis of the Putative Succinyl-Diaminopimelic Acid Desuccinylase DapE from Campylobacter jejuni: Captopril-Mediated Structural Stabilization by Si Yeon Ahn, Young-Bong You, Han Byeol Oh, Min-Ah Park, Sung-il Yoon, Guangfeng Zhou (2025) 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-12731327.txt.
Description
Ahn and co-authors solved, in a 2025 structural study, the shape of a bacterial enzyme that drug designers hope to block. They also caught the blood pressure drug captopril holding it still. The enzyme, DapE, builds a brick the cell wall cannot do without. Humans lack the pathway, making it a clean target. Their subject was the version from Campylobacter jejuni, a food poisoning culprit.
Crystal snapshots show a two-part enzyme that pairs into a dimer, with two zinc ions at its working pocket. Without the drug, two loops of the pairing region hang loose. Captopril binding snaps them into order and wedges the enzyme open, a pose that cannot work. The pictures explain the block as simple competition for the substrate's seat.
Catalog record
| CREATOR | Si Yeon Ahn, Young-Bong You, Han Byeol Oh, Min-Ah Park, Sung-il Yoon, Guangfeng Zhou |
|---|---|
| YEAR | 2025 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 33 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |