6Y1Y

CheA dimerization domain of Treponema denticola

Summary for 6Y1Y

• Entry DOI: 10.2210/pdb6y1y/pdb
• Descriptor: CheA (2 entities in total)
• Functional Keywords: histidine kinase, dimerization domain, coiled-coil, signaling protein
• Biological source: Treponema denticola
• Total number of polymer chains: 2
• Total formula weight: 29595.73

Authors

Muok, A.R.,Briegel, A.,Crane, B.R. (deposition date: 2020-02-14, release date: 2020-10-28, Last modification date: 2024-05-15)

Primary citation

Muok, A.R.,Ortega, D.R.,Kurniyati, K.,Yang, W.,Maschmann, Z.A.,Sidi Mabrouk, A.,Li, C.,Crane, B.R.,Briegel, A.
Atypical chemoreceptor arrays accommodate high membrane curvature.
Nat Commun, 11:5763-5763, 2020

PubMed Abstract: The prokaryotic chemotaxis system is arguably the best-understood signaling pathway in biology. In all previously described species, chemoreceptors organize into a hexagonal (P6 symmetry) extended array. Here, we report an alternative symmetry (P2) of the chemotaxis apparatus that emerges from a strict linear organization of the histidine kinase CheA in Treponema denticola cells, which possesses arrays with the highest native curvature investigated thus far. Using cryo-ET, we reveal that Td chemoreceptor arrays assume an unusual arrangement of the supra-molecular protein assembly that has likely evolved to accommodate the high membrane curvature. The arrays have several atypical features, such as an extended dimerization domain of CheA and a variant CheW-CheR-like fusion protein that is critical for maintaining an ordered chemosensory apparatus. Furthermore, the previously characterized Td oxygen sensor ODP influences CheA ordering. These results suggest a greater diversity of the chemotaxis signaling system than previously thought.

PubMed: 33188180
DOI: 10.1038/s41467-020-19628-6

Experimental method

X-RAY DIFFRACTION (1.5 Å)