A chemotactic signaling surface on CheY defined by suppressors of flagellar switch mutations.
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CHEMOTAXIS-GUIDED MOVEMENTS IN BACTERIACorrelated switch binding and signaling in bacterial chemotaxisA distinct meta-active conformation in the 1.1-A resolution structure of wild-type ApoCheYThe structures of T87I phosphono-CheY and T87I/Y106W phosphono-CheY help to explain their binding affinities to the FliM and CheZ peptidesStructure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thalianaUncoupled phosphorylation and activation in bacterial chemotaxis. The 2.1-A structure of a threonine to isoleucine mutant at position 87 of CheYCrystal structures of CheY mutants Y106W and T87I/Y106W. CheY activation correlates with movement of residue 106Uncoupled phosphorylation and activation in bacterial chemotaxis. The 2.3 A structure of an aspartate to lysine mutant at position 13 of CheYTwo binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathwayAn ABC transporter plays a developmental aggregation role in Myxococcus xanthus.The Type IX Secretion System (T9SS): Highlights and Recent Insights into Its Structure and Function.Proposed signal transduction role for conserved CheY residue Thr87, a member of the response regulator active-site quintet.Computer-aided resolution of an experimental paradox in bacterial chemotaxis.Activation of the phosphosignaling protein CheY. II. Analysis of activated mutants by 19F NMR and protein engineeringThe two-component signaling pathway of bacterial chemotaxis: a molecular view of signal transduction by receptors, kinases, and adaptation enzymesActivation of the phosphosignaling protein CheY. I. Analysis of the phosphorylated conformation by 19F NMR and protein engineeringExcitatory signaling in bacterial probed by caged chemoeffectorsLiberation of an interaction domain from the phosphotransfer region of CheA, a signaling kinase of Escherichia coli.FliG and FliM distribution in the Salmonella typhimurium cell and flagellar basal bodies.Tyrosine 106 of CheY plays an important role in chemotaxis signal transduction in Escherichia coli.In vivo and in vitro characterization of Escherichia coli protein CheZ gain- and loss-of-function mutants.Isolation and characterization of rcsB mutations that affect colanic acid capsule synthesis in Escherichia coli K-12.Analysis of a chemotaxis operon from Rhodospirillum centenum.Conformational coupling in the chemotaxis response regulator CheY.Acetylation at Lys-92 enhances signaling by the chemotaxis response regulator protein CheY.Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced thermostability.Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteriaFunctions of the gene products of Escherichia coli.The PorX Response Regulator of the Porphyromonas gingivalis PorXY Two-Component System Does Not Directly Regulate the Type IX Secretion Genes but Binds the PorL SubunitAccumulation of Peptidoglycan O-Acetylation Leads to Altered Cell Wall Biochemistry and Negatively Impacts Pathogenesis Factors of Campylobacter jejuni.Isolation and in vitro characterization of CheZ suppressors for the Escherichia coli chemotactic response regulator mutant CheYN23D.Analysis of a FliM-FliN flagellar switch fusion mutant of Salmonella typhimurium.Salmonella typhimurium fliG and fliN mutations causing defects in assembly, rotation, and switching of the flagellar motor.Gene to ultrastructure: the case of the flagellar basal body.The pilG gene product, required for Pseudomonas aeruginosa pilus production and twitching motility, is homologous to the enteric, single-domain response regulator CheY.Only one of the five CheY homologs in Vibrio cholerae directly switches flagellar rotationIdentification of communication networks in Spo0F: a model for phosphorylation-induced conformational change and implications for activation of multiple domain bacterial response regulators.1H, 15N, and 13C backbone chemical shift assignments, secondary structure, and magnesium-binding characteristics of the Bacillus subtilis response regulator, Spo0F, determined by heteronuclear high-resolution NMR.Flagellar motor-switch binding face of CheY and the biochemical basis of suppression by CheY mutants that compensate for motor-switch defects in Escherichia coli.The bidirectional polar and unidirectional lateral flagellar motors of Vibrio alginolyticus are controlled by a single CheY species.
P2860
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P2860
A chemotactic signaling surface on CheY defined by suppressors of flagellar switch mutations.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
A chemotactic signaling surfac ...... of flagellar switch mutations.
@en
A chemotactic signaling surfac ...... of flagellar switch mutations.
@nl
type
label
A chemotactic signaling surfac ...... of flagellar switch mutations.
@en
A chemotactic signaling surfac ...... of flagellar switch mutations.
@nl
prefLabel
A chemotactic signaling surfac ...... of flagellar switch mutations.
@en
A chemotactic signaling surfac ...... of flagellar switch mutations.
@nl
P2093
P2860
P1476
A chemotactic signaling surfac ...... of flagellar switch mutations.
@en
P2093
P2860
P304
P356
10.1128/JB.174.19.6247-6255.1992
P577
1992-10-01T00:00:00Z