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. 2021 Mar 25;11(4):495. doi: 10.3390/biom11040495

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© 2021 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Difference in the intermolecular distance and the relative orientation of neighbouring CheA molecules between p6 and p2 chemosensory array architectures. (A) The p6 architecture. (B) The p2 architecture. Rough distances between a given CheA monomer, as measured from the end of the P2-P3 linker (residue I264), and ATP-binding sites on neighbouring CheAs that may be accessible in a trans-fashion by the associated P1 domain (dashed lines). The CheA.P1 and CheA.P2 domains are modelled for a centralized CheA dimer and shown in green. The ATP lid (residues 455–475) of each CheA monomer is shown in purple. Receptors, CheW, and CheA.P5 are not shown for clarity.