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-Structure paper
Title | Atypical chemoreceptor arrays accommodate high membrane curvature. |
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Journal, issue, pages | Nat Commun, Vol. 11, Issue 1, Page 5763, Year 2020 |
Publish date | Nov 13, 2020 |
Authors | Alise R Muok / Davi R Ortega / Kurni Kurniyati / Wen Yang / Zachary A Maschmann / Adam Sidi Mabrouk / Chunhao Li / Brian R Crane / Ariane Briegel / |
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 ...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. |
External links | Nat Commun / PubMed:33188180 / PubMed Central |
Methods | EM (subtomogram averaging) / EM (tomography) / X-ray diffraction |
Resolution | 1.5 - 46.0 Å |
Structure data | EMDB-11381: EMDB-11384: EMDB-11385: EMDB-11386: PDB-6y1y: |
Chemicals | ChemComp-HOH: |
Source |
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Keywords | SIGNALING PROTEIN / Histidine kinase / dimerization domain / coiled-coil |