Bibliographic Details
| Title: |
Mechanism of sensor kinase CitA transmembrane signaling |
| Authors: |
Xizhou Cecily Zhang, Kai Xue, Michele Salvi, Benjamin Schomburg, Jonas Mehrens, Karin Giller, Marius Stopp, Siegfried Weisenburger, Daniel Böning, Vahid Sandoghdar, Gottfried Unden, Stefan Becker, Loren B. Andreas, Christian Griesinger |
| Source: |
Nature Communications, Vol 16, Iss 1, Pp 1-11 (2025) |
| Publisher Information: |
Nature Portfolio, 2025. |
| Publication Year: |
2025 |
| Collection: |
LCC:Science |
| Subject Terms: |
Science |
| More Details: |
Abstract Membrane bound histidine kinases (HKs) are ubiquitous sensors of extracellular stimuli in bacteria. However, a uniform structural model is still missing for their transmembrane signaling mechanism. Here, we used solid-state NMR in conjunction with crystallography, solution NMR and distance measurements to investigate the transmembrane signaling mechanism of a paradigmatic citrate sensing membrane embedded HK, CitA. Citrate binding in the sensory extracytoplasmic PAS domain (PASp) causes the linker to transmembrane helix 2 (TM2) to adopt a helical conformation. This triggers a piston-like pulling of TM2 and a quaternary structure rearrangement in the cytosolic PAS domain (PASc). Crystal structures of PASc reveal both anti-parallel and parallel dimer conformations. An anti-parallel to parallel transition upon citrate binding agrees with interdimer distances measured in the lipid embedded protein using a site-specific 19F label in PASc. These data show how Angstrom scale structural changes in the sensor domain are transmitted across the membrane to be converted and amplified into a nm scale shift in the linker to the phosphorylation subdomain of the kinase. |
| Document Type: |
article |
| File Description: |
electronic resource |
| Language: |
English |
| ISSN: |
2041-1723 |
| Relation: |
https://doaj.org/toc/2041-1723 |
| DOI: |
10.1038/s41467-024-55671-3 |
| Access URL: |
https://doaj.org/article/6d5a6bc4743b46c2baa5ffdd20fe3cd4 |
| Accession Number: |
edsdoj.6d5a6bc4743b46c2baa5ffdd20fe3cd4 |
| Database: |
Directory of Open Access Journals |
