Dynamic domain interactions encode possible CheA autophosphorylation mechanisms revealed by coarse-grained simulations.

ABSTRACT: Autophosphorylation of CheA is key to initiation of the phosphorylation cascade that eventually controls the direction of downstream flagellar motors for chemotaxis signaling in motile bacteria. The phospho-transfer reaction, from ATP bound in the P4 catalytic domain to a specific His residue in the P1 substrate domain in CheA, can be significantly accelerated within core signaling unit complexes containing chemoreceptors, CheA and CheW. Previous studies have proposed that CheA autophosphorylation activity is regulated by changing the dynamics of P4 and/or altering its interactions with P1 in response to signals transmitted from chemoreceptors. However, the positions of CheA P1 and P2 domains in the core signaling unit are not well-characterized because they form only transient interaction

SUBMITTER: Huang J 

PROVIDER: S-EPMC12767644 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature