- EMDB-5549: Signaling in Chemoreceptor Arrays Through Mobility Control of Kin... -
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データベース: EMDB / ID: EMD-5549
タイトル
Signaling in Chemoreceptor Arrays Through Mobility Control of Kinase Domains - kinase activity state locked off - tsr mutant A413T, deletion of subdomains P1 and P2 from CheA
マップデータ
Subvolume average chemoreceptor mutant tsr A413T/CheA mutant deltaP1P2/CheW
試料
試料: chemoreceptor array with mutant receptor tsr A413T CheA mutant delta P1P2
ジャーナル: Mol Microbiol / 年: 2013 タイトル: The mobility of two kinase domains in the Escherichia coli chemoreceptor array varies with signalling state. 著者: Ariane Briegel / Peter Ames / James C Gumbart / Catherine M Oikonomou / John S Parkinson / Grant J Jensen / 要旨: Motile bacteria sense their physical and chemical environment through highly cooperative, ordered arrays of chemoreceptors. These signalling complexes phosphorylate a response regulator which in turn ...Motile bacteria sense their physical and chemical environment through highly cooperative, ordered arrays of chemoreceptors. These signalling complexes phosphorylate a response regulator which in turn governs flagellar motor reversals, driving cells towards favourable environments. The structural changes that translate chemoeffector binding into the appropriate kinase output are not known. Here, we apply high-resolution electron cryotomography to visualize mutant chemoreceptor signalling arrays in well-defined kinase activity states. The arrays were well ordered in all signalling states, with no discernible differences in receptor conformation at 2-3 nm resolution. Differences were observed, however, in a keel-like density that we identify here as CheA kinase domains P1 and P2, the phosphorylation site domain and the binding domain for response regulator target proteins. Mutant receptor arrays with high kinase activities all exhibited small keels and high proteolysis susceptibility, indicative of mobile P1 and P2 domains. In contrast, arrays in kinase-off signalling states exhibited a range of keel sizes. These findings confirm that chemoreceptor arrays do not undergo large structural changes during signalling, and suggest instead that kinase activity is modulated at least in part by changes in the mobility of key domains.