8BJP
The N288D mutant cytoplasmic PAS domain of Geobacillus thermodenitrificans histidine kinase CitA
This is a non-PDB format compatible entry.
Summary for 8BJP
| Entry DOI | 10.2210/pdb8bjp/pdb |
| Descriptor | cytoplasmic PAS domain of CitA from Geobacillus thermodenitrificans, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | cytoplasmic pas domain, cita, histidine kinase, transmembrane signaling, signaling protein |
| Biological source | Geobacillus thermodenitrificans |
| Total number of polymer chains | 2 |
| Total formula weight | 24916.10 |
| Authors | Becker, S. (deposition date: 2022-11-04, release date: 2023-11-15, Last modification date: 2025-05-21) |
| Primary citation | Zhang, X.C.,Xue, K.,Salvi, M.,Schomburg, B.,Mehrens, J.,Giller, K.,Stopp, M.,Weisenburger, S.,Boning, D.,Sandoghdar, V.,Unden, G.,Becker, S.,Andreas, L.B.,Griesinger, C. Mechanism of sensor kinase CitA transmembrane signaling. Nat Commun, 16:935-935, 2025 Cited by PubMed 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 F 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. PubMed: 39843904DOI: 10.1038/s41467-024-55671-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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