Conformational dynamics of the membrane-anchored foldase LipH from Pseudomonas aeruginosa governs recognition and release of its client lipase
Max Busch, Jennifer Loschwitz, Athanasios Papadopoulos, Jens Reiners, Wieland Steinchen, Vincenzo Calvagna, Sander H.J. Smits, Karl-Erich Jaeger, Alexej Kedrov · 2026
Read Conformational dynamics of the membrane-anchored foldase LipH from Pseudomonas aeruginosa governs recognition and release of its client lipase by Max Busch, Jennifer Loschwitz, Athanasios Papadopoulos, Jens Reiners, Wieland Steinchen, Vincenzo Calvagna, Sander H.J. Smits, Karl-Erich Jaeger, Alexej Kedrov (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/PMC13381987.txt.
Description
Max Busch and co-authors present a 2026 study of a helper protein that folds a bacterial enzyme before the bacterium exports it. The bacterium, Pseudomonas aeruginosa, causes infections, and the enzyme it exports helps it do harm. The helper, called LipH, sits anchored in the cell membrane, and its working motions were barely understood.
Computer simulations showed the anchored helper is highly flexible, sweeping through many shapes. Its working cavity is sometimes blocked by the membrane itself or by its own linker section. Despite that, lab tests with the helper rebuilt into artificial membranes showed it still activates its client enzyme efficiently. The picture explains how a tethered folding helper can catch and release its target.
Catalog record
| CREATOR | Max Busch, Jennifer Loschwitz, Athanasios Papadopoulos, Jens Reiners, Wieland Steinchen, Vincenzo Calvagna, Sander H.J. Smits, Karl-Erich Jaeger, Alexej Kedrov |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 80263 |
| LICENSE | https://creativecommons.org/licenses/by/4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |