Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	The mobility of two kinase domains in the Escherichia coli chemoreceptor array varies with signalling state.
Journal, issue, pages	Mol Microbiol, Vol. 89, Issue 5, Page 831-841, Year 2013
Publish date	Jul 30, 2013
Authors	Ariane Briegel / Peter Ames / James C Gumbart / Catherine M Oikonomou / John S Parkinson / Grant J Jensen /
PubMed Abstract	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.
External links	Mol Microbiol / PubMed:23802570 / PubMed Central
Methods	EM (subtomogram averaging)
Resolution	25.0 - 32.0 Å
Structure data	EMDB-2414: Signaling in Chemoreceptor Arrays Through Mobility Control of Kinase Domains - kinase activity state locked off - tsr mutant M222R Method: EM (subtomogram averaging) / Resolution: 30.0 Å EMDB-5541: Signaling in Chemoreceptor Arrays Through Mobility Control of Kinase Domains - kinase activity state locked off - tsr mutant A413T Method: EM (subtomogram averaging) / Resolution: 25.0 Å EMDB-5542: Signaling in Chemoreceptor Arrays Through Mobility Control of Kinase Domains - low kinase activity state - tsr mutant P221D Method: EM (subtomogram averaging) / Resolution: 25.0 Å EMDB-5543: Signaling in Chemoreceptor Arrays Through Mobility Control of Kinase Domains - low kinase activity state - tsr mutant EEEE Method: EM (subtomogram averaging) / Resolution: 25.0 Å EMDB-5545: Signaling in Chemoreceptor Arrays Through Mobility Control of Kinase Domains - high kinase activity state - tsr mutant QQQQ Method: EM (subtomogram averaging) / Resolution: 25.0 Å EMDB-5546: Signaling in Chemoreceptor Arrays Through Mobility Control of Kinase Domains - kinase activity state locked on - tsr mutant I241E Method: EM (subtomogram averaging) / Resolution: 25.0 Å EMDB-5547: Signaling in Chemoreceptor Arrays Through Mobility Control of Kinase Domains - kinase activity state locked on - tsr mutant G235E Method: EM (subtomogram averaging) / Resolution: 25.0 Å EMDB-5548: Signaling in Chemoreceptor Arrays Through Mobility Control of Kinase Domains - high kinase activity state - tsr mutant QEQE Method: EM (subtomogram averaging) / Resolution: 25.0 Å EMDB-5549: 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 Method: EM (subtomogram averaging) / Resolution: 25.0 Å EMDB-5550: Signaling in Chemoreceptor Arrays Through Mobility Control of Kinase Domains - kinase activity state locked off - tsr mutant A413T, subdomain P2 deleted from CheA Method: EM (subtomogram averaging) / Resolution: 25.0 Å EMDB-5716: Signaling in Chemoreceptor Arrays Through Mobility Control of Kinase Domains - kinase activity state locked off - tsr variant P221DdeltaP1P2 Method: EM (subtomogram averaging) / Resolution: 32.0 Å
Source	Escherichia coli (E. coli)