Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface
about
Use of 19F NMR to probe protein structure and conformational changesHelix cappingRapid radiation in bacteria leads to a division of labourCrystallographic and biochemical studies of DivK reveal novel features of an essential response regulator in Caulobacter crescentusThe X-ray Crystal Structures of Two Constitutively Active Mutants of the Escherichia coli PhoB Receiver Domain Give Insights into ActivationThe structure of a full-length response regulator from Mycobacterium tuberculosis in a stabilized three-dimensional domain-swapped, activated stateBasis of Mutual Domain Inhibition in a Bacterial Response RegulatorUncoupled 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 CheYCrystal structures of the copper and nickel complexes of RNase A: metal-induced interprotein interactions and identification of a novel copper binding motifTwo binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathwayThe structural basis of signal transduction for the response regulator PrrA from Mycobacterium tuberculosisIdentification of the histidine protein kinase KinB in Pseudomonas aeruginosa and its phosphorylation of the alginate regulator algBCrystal structures of two cyanobacterial response regulators in apo- and phosphorylated form reveal a novel dimerization motif of phytochrome-associated response regulators.How evolution makes proteins fold quicklyDistinguishing multiple chemotaxis Y protein conformations with laser-polarized 129Xe NMR.The two-component signaling pathway of bacterial chemotaxis: a molecular view of signal transduction by receptors, kinases, and adaptation enzymesThe VirR response regulator from Clostridium perfringens binds independently to two imperfect direct repeats located upstream of the pfoA promoterRelationship between ion pair geometries and electrostatic strengths in proteins.Conformational changes of Spo0F along the phosphotransfer pathway.Tuning magnesium sensitivity of BK channels by mutations.Pleiotropic phenotypes caused by genetic ablation of the receiver module of the Agrobacterium tumefaciens VirA proteinConformational Dynamics of Response Regulator RegX3 from Mycobacterium tuberculosis.Acetylation at Lys-92 enhances signaling by the chemotaxis response regulator protein CheY.Investigation of the role of electrostatic charge in activation of the Escherichia coli response regulator CheY.Altered recognition mutants of the response regulator PhoB: a new genetic strategy for studying protein-protein interactions.Characterisation of the isolated Che Y C-terminal fragment (79-129)--Exploring the structure/stability/folding relationship of the alpha/beta parallel protein Che Y.Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active statesAnalysis of the conserved acidic residues in the regulatory domain of PhoB.Conformational dynamics as a key factor of signaling mediated by the receiver domain of sensor histidine kinase from Arabidopsis thaliana.Switched or not?: the structure of unphosphorylated CheY bound to the N terminus of FliM.Ligand-induced folding of a two-component signaling receiver domain.Identification of the Mg2+-binding site in the P-type ATPase and phosphatase members of the HAD (haloacid dehalogenase) superfamily by structural similarity to the response regulator protein CheY.The distribution of alpha-helix propensity along the polypeptide chain is not conserved in proteins from the same familySegmental motions, not a two-state concerted switch, underlie allostery in CheY.Insights into correlated motions and long-range interactions in CheY derived from molecular dynamics simulations.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.Alteration of a nonconserved active site residue in the chemotaxis response regulator CheY affects phosphorylation and interaction with CheZ.Importance of Thr-353 of the conserved phosphorylation loop of the sarcoplasmic reticulum Ca2+-ATPase in MgATP binding and catalytic activity.
P2860
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P2860
Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface
description
1994 nî lūn-bûn
@nan
1994 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Magnesium binding to the bacte ...... volving its functional surface
@ast
Magnesium binding to the bacte ...... volving its functional surface
@en
Magnesium binding to the bacte ...... volving its functional surface
@nl
type
label
Magnesium binding to the bacte ...... volving its functional surface
@ast
Magnesium binding to the bacte ...... volving its functional surface
@en
Magnesium binding to the bacte ...... volving its functional surface
@nl
prefLabel
Magnesium binding to the bacte ...... volving its functional surface
@ast
Magnesium binding to the bacte ...... volving its functional surface
@en
Magnesium binding to the bacte ...... volving its functional surface
@nl
P2093
P356
P1476
Magnesium binding to the bacte ...... volving its functional surface
@en
P2093
P304
P356
10.1006/JMBI.1994.1308
P50
P577
1994-05-01T00:00:00Z