Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY
about
Structure and function from the circadian clock protein KaiA of Synechococcus elongatus: a potential clock input mechanism.Crystal structure of the CheA histidine phosphotransfer domain that mediates response regulator phosphorylation in bacterial chemotaxisA 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 interfaceCrystal structure of a phosphatase with a unique substrate binding domain fromThermotoga maritimaStructural insight into the low affinity between Thermotoga maritima CheA and CheB compared to their Escherichia coli/Salmonella typhimurium counterpartsThe 3.2 Å Resolution Structure of a Receptor:CheA:CheW Signaling Complex Defines Overlapping Binding Sites and Key Residue Interactions within Bacterial Chemosensory ArraysSolution Structure of a Complex of the Histidine Autokinase CheA with Its Substrate CheYTwo binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathwayMaking sense of it all: bacterial chemotaxisDefining 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 histidine kinase domain of UhpB inhibits UhpA action at the Escherichia coli uhpT promoter.The phosphoryl transfer domain of UhpB interacts with the response regulator UhpA.Crystal structures of two cyanobacterial response regulators in apo- and phosphorylated form reveal a novel dimerization motif of phytochrome-associated response regulators.Phosphorylation of proteins in the light-dependent signalling pathway of a filamentous cyanobacterium.Inhibitors of bacterial two-component signalling systems.The two active sites of Thermotoga maritima CheA dimers bind ATP with dramatically different affinitiesMultiple mechanisms of action for inhibitors of histidine protein kinases from bacterial two-component systems.The structure of a cyanobacterial sucrose-phosphatase reveals the sugar tongs that release free sucrose in the cell.How signals are heard during bacterial chemotaxis: protein-protein interactions in sensory signal propagation.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 changes of Spo0F along the phosphotransfer pathway.Fungal histidine kinases.Self-assembly of receptor/signaling complexes in bacterial chemotaxisIdentification of an anchor residue for CheA-CheY interactions in the chemotaxis system of Escherichia coli.Purification, crystallization and preliminary X-ray diffraction analysis of human enolase-phosphatase E1.Conformational coupling in the chemotaxis response regulator CheY.Crystal structure of trehalose-6-phosphate phosphatase-related protein: biochemical and biological implicationsGenetic 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.In different organisms, the mode of interaction between two signaling proteins is not necessarily conserved.Three-dimensional structure and organization of a receptor/signaling complex.Conformational dynamics as a key factor of signaling mediated by the receiver domain of sensor histidine kinase from Arabidopsis thaliana.Different evolutionary constraints on chemotaxis proteins CheW and CheY revealed by heterologous expression studies and protein sequence analysis.Crystal structure of the response regulator 02 receiver domain, the essential YycF two-component system of Streptococcus pneumoniae in both complexed and native states.Protein-protein interactions as a tool for site-specific labeling of proteins.Organization of the receptor-kinase signaling array that regulates Escherichia coli chemotaxis.Subunit organization in a soluble complex of tar, CheW, and CheA by electron microscopy.Two transcriptional regulators GlnR and GlnRII are involved in regulation of nitrogen metabolism in Streptomyces coelicolor A3(2).Dynamic domain arrangement of CheA-CheY complex regulates bacterial thermotaxis, as revealed by NMR.
P2860
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P2860
Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY
description
1998 nî lūn-bûn
@nan
1998 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
name
Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY
@ast
Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY
@en
Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY
@nl
type
label
Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY
@ast
Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY
@en
Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY
@nl
prefLabel
Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY
@ast
Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY
@en
Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY
@nl
P2093
P2860
P356
P1476
Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY
@en
P2093
P2860
P2888
P356
10.1038/NSB0198-25
P577
1998-01-01T00:00:00Z
P5875
P6179
1016305076