Affiliation:
1. School of Biological Sciences, University of Utah, Salt Lake City, Utah, USA
Abstract
Regulation of CheA kinase in chemoreceptor arrays is critical for
Escherichia coli
chemotaxis. However, to date, little is known about the CheA conformations that lead to the kinase-on or kinase-off states. Here, we explore the signaling roles of a distinct conformation of the ATP-binding CheA.P4 domain identified by all-atom molecular dynamics simulation. Amino acid replacements at residues predicted to stabilize the so-called “dipped” CheA.P4 conformation abolished the kinase activity of CheA and its ability to support chemotaxis. Our findings indicate that the dipped conformation of the CheA.P4 domain is critical for reaching the kinase-active state in chemoreceptor signaling arrays.
Funder
HHS | NIH | National Institute of General Medical Sciences
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
12 articles.
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