Thermal domain motions of CheA kinase in solution: Disulfide trapping reveals the motional constraints leading to trans-autophosphorylation
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Defining a key receptor-CheA kinase contact and elucidating its function in the membrane-bound bacterial chemosensory array: a disulfide mapping and TAM-IDS Study.The two active sites of Thermotoga maritima CheA dimers bind ATP with dramatically different affinitiesProtein histidine kinases: assembly of active sites and their regulation in signaling pathways.Structure of the ternary complex formed by a chemotaxis receptor signaling domain, the CheA histidine kinase, and the coupling protein CheW as determined by pulsed dipolar ESR spectroscopy.Conformational Transitions that Enable Histidine Kinase Autophosphorylation and Receptor Array Integration.Mutational analysis of the P1 phosphorylation domain in Escherichia coli CheA, the signaling kinase for chemotaxis.The linker between the dimerization and catalytic domains of the CheA histidine kinase propagates changes in structure and dynamics that are important for enzymatic activityIsolated bacterial chemosensory array possesses quasi- and ultrastable components: functional links between array stability, cooperativity, and order.Computational and experimental analyses reveal the essential roles of interdomain linkers in the biological function of chemotaxis histidine kinase CheA.Structure, function, and on-off switching of a core unit contact between CheA kinase and CheW adaptor protein in the bacterial chemosensory array: A disulfide mapping and mutagenesis studyEngineered socket study of signaling through a four-helix bundle: evidence for a yin-yang mechanism in the kinase control module of the aspartate receptor.
P2860
Q30009859-4AFD58BE-C18F-4276-A7F4-EB59C9DDCC8BQ33609827-F050BB5C-885B-40A3-BB81-58D68277AFD5Q33762077-7B7DC0AA-2ED3-4842-B78A-613C3769262EQ34107640-4BC49973-88EA-47ED-818A-089BB8BD408BQ36486040-F0CA1B17-DAA6-4FC3-B7B2-CB65BEC61900Q37545917-18EFED0B-A282-4AF4-AA1C-43B43CE9BE2BQ38736598-37CD3948-FD35-4960-BA6B-3D4842FD4B88Q39297839-88DDD5EC-2B89-4FD0-B065-4039D7879C93Q41668268-3FE367C0-14A8-4434-ADAF-1D836944010FQ41888519-4222F7C6-2662-42D7-8370-B42FD2ED8C65Q42116099-2AA40694-C84E-4CDA-A7D0-5F2937F99089
P2860
Thermal domain motions of CheA kinase in solution: Disulfide trapping reveals the motional constraints leading to trans-autophosphorylation
description
2009 nî lūn-bûn
@nan
2009 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年学术文章
@wuu
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
@yue
name
Thermal domain motions of CheA ...... g to trans-autophosphorylation
@ast
Thermal domain motions of CheA ...... g to trans-autophosphorylation
@en
type
label
Thermal domain motions of CheA ...... g to trans-autophosphorylation
@ast
Thermal domain motions of CheA ...... g to trans-autophosphorylation
@en
prefLabel
Thermal domain motions of CheA ...... g to trans-autophosphorylation
@ast
Thermal domain motions of CheA ...... g to trans-autophosphorylation
@en
P2860
P356
P1433
P1476
Thermal domain motions of CheA ...... g to trans-autophosphorylation
@en
P2093
Joseph J Falke
Susan L Gloor
P2860
P304
P356
10.1021/BI900033R
P407
P577
2009-04-01T00:00:00Z