The 1.9 A resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY
about
BeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate: structure of a BeF(3)(-) complex with phosphoserine phosphataseProkaryotic 2-component systems and the OmpR/PhoB superfamilyCrystal structure of activated CheY. Comparison with other activated receiver domainsA distinct meta-active conformation in the 1.1-A resolution structure of wild-type ApoCheYThe crystal structure of the phosphorylation domain in PhoP reveals a functional tandem association mediated by an asymmetric interfaceStructure of an atypical orphan response regulator protein supports a new phosphorylation-independent regulatory mechanismDomain Orientation in the Inactive Response Regulator Mycobacterium tuberculosis MtrA Provides a Barrier to Activation † , ‡The structures of T87I phosphono-CheY and T87I/Y106W phosphono-CheY help to explain their binding affinities to the FliM and CheZ peptidesInsights into Aurora-A Kinase Activation Using Unnatural Amino Acids Incorporated by Chemical ModificationPhosphorylated Ssk1 prevents unphosphorylated Ssk1 from activating the Ssk2 mitogen-activated protein kinase kinase kinase in the yeast high-osmolarity glycerol osmoregulatory pathwayDiverse functionalization of Aurora-A kinase at specified surface and buried sites by native chemical modificationMaking sense of it all: bacterial chemotaxisChemotaxis signaling protein CheY binds to the rotor protein FliN to control the direction of flagellar rotation in Escherichia coli.Genetic evidence that the alpha5 helix of the receiver domain of PhoB is involved in interdomain interactionsHow signals are heard during bacterial chemotaxis: protein-protein interactions in sensory signal propagation.Genetic analysis of response regulator activation in bacterial chemotaxis suggests an intermolecular mechanism.Crystal structures of beryllium fluoride-free and beryllium fluoride-bound CheY in complex with the conserved C-terminal peptide of CheZ reveal dual binding modes specific to CheY conformation.Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active statesStructural analysis and solution studies of the activated regulatory domain of the response regulator ArcA: a symmetric dimer mediated by the alpha4-beta5-alpha5 face.Biological insights from structures of two-component proteins.Molecular dynamics of the FixJ receiver domain: movement of the beta4-alpha4 loop correlates with the in and out flip of Phe101.Switched or not?: the structure of unphosphorylated CheY bound to the N terminus of FliM.Evidence against the "Y-T coupling" mechanism of activation in the response regulator NtrC.Involvement of Two-Component Signaling on Bacterial Motility and Biofilm Development.Production, characterization, and assessment of a stable analog of the response regulator CheY-phosphate from Thermotoga maritima.
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P2860
The 1.9 A resolution crystal structure of phosphono-CheY, an analogue of the active form of the response regulator, CheY
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The 1.9 A resolution crystal s ...... f the response regulator, CheY
@ast
The 1.9 A resolution crystal s ...... f the response regulator, CheY
@en
The 1.9 A resolution crystal s ...... f the response regulator, CheY
@nl
type
label
The 1.9 A resolution crystal s ...... f the response regulator, CheY
@ast
The 1.9 A resolution crystal s ...... f the response regulator, CheY
@en
The 1.9 A resolution crystal s ...... f the response regulator, CheY
@nl
prefLabel
The 1.9 A resolution crystal s ...... f the response regulator, CheY
@ast
The 1.9 A resolution crystal s ...... f the response regulator, CheY
@en
The 1.9 A resolution crystal s ...... f the response regulator, CheY
@nl
P2093
P356
P1433
P1476
The 1.9 A resolution crystal s ...... f the response regulator, CheY
@en
P2093
C J Halkides
F W Dahlquist
M M McEvoy
P Matsumura
P304
P356
10.1021/BI9925524
P407
P577
2000-05-09T00:00:00Z