A distinct meta-active conformation in the 1.1-A resolution structure of wild-type ApoCheY
about
Structure and function from the circadian clock protein KaiA of Synechococcus elongatus: a potential clock input mechanism.Structure of an atypical orphan response regulator protein supports a new phosphorylation-independent regulatory mechanismAn atypical receiver domain controls the dynamic polar localization of the Myxococcus xanthus social motility protein FrzSCrystal Structures of the Response Regulator DosR from Mycobacterium tuberculosis Suggest a Helix Rearrangement Mechanism for Phosphorylation ActivationThe structures of T87I phosphono-CheY and T87I/Y106W phosphono-CheY help to explain their binding affinities to the FliM and CheZ peptidesMatching Biochemical Reaction Kinetics to the Timescales of Life: Structural Determinants That Influence the Autodephosphorylation Rate of Response Regulator ProteinsRegulation of Response Regulator Autophosphorylation through Interdomain ContactsStructural Basis of Response Regulator Dephosphorylation by Rap PhosphatasesAn asymmetric heterodomain interface stabilizes a response regulator–DNA complexAnalysis of protein hydration in ultrahigh-resolution structures of the SRP GTPase FfhDistinguishing multiple chemotaxis Y protein conformations with laser-polarized 129Xe NMR.Contrasting roles of dynamics in protein allostery: NMR and structural studies of CheY and the third PDZ domain from PSD-95.Receiver domain structure and function in response regulator proteins.Entropic mechanism of large fluctuation in allosteric transition.Allostery and cooperativity revisited.A theory of protein dynamics to predict NMR relaxationInvestigation of the role of electrostatic charge in activation of the Escherichia coli response regulator CheY.Genetic analysis of response regulator activation in bacterial chemotaxis suggests an intermolecular mechanism.Bacterial response regulators: versatile regulatory strategies from common domains.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.Activation mechanism of a signaling protein at atomic resolution from advanced computationsColocalization of fast and slow timescale dynamics in the allosteric signaling protein CheYProbing the roles of the two different dimers mediated by the receiver domain of the response regulator PhoB.Single domain response regulators: molecular switches with emerging roles in cell organization and dynamicsMolecular dynamics of the FixJ receiver domain: movement of the beta4-alpha4 loop correlates with the in and out flip of Phe101.Conformational dynamics as a key factor of signaling mediated by the receiver domain of sensor histidine kinase from Arabidopsis thaliana.A new perspective on response regulator activation.Switched or not?: the structure of unphosphorylated CheY bound to the N terminus of FliM.Use of restrained molecular dynamics to predict the conformations of phosphorylated receiver domains in two-component signaling systems.Topological frustration in beta alpha-repeat proteins: sequence diversity modulates the conserved folding mechanisms of alpha/beta/alpha sandwich proteins.Constitutive activation of two-component response regulators: characterization of VirG activation in Agrobacterium tumefaciens.Segmental 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.Allosteric activation of bacterial response regulators: the role of the cognate histidine kinase beyond phosphorylation.Evidence against the "Y-T coupling" mechanism of activation in the response regulator NtrC.Structural complementarity of Toll/interleukin-1 receptor domains in Toll-like receptors and the adaptors Mal and MyD88.
P2860
Q24539011-18CC39F0-6C71-406B-AE5B-BC637FE35015Q27644734-957F9451-5D84-43BF-928C-92B9C7083524Q27645973-3E805773-5093-4CBC-AF32-762C5816BD77Q27650110-1DC43DDB-351B-4191-BBC5-7613531E5746Q27652225-D7937E11-D494-447E-BE2F-788E26FCA17FQ27656808-D26F47DA-072B-40C7-9EE9-C9A2CE96704DQ27664032-81CF8D6E-1198-49EB-A556-C23948B4FF94Q27667042-7ADBF8FF-5EF9-4C59-A1C6-4A25A0512B06Q27681718-78792BEB-6B9C-422B-B92D-FAF98A63FF6AQ30358425-75D565EF-4992-444B-A3C0-356D965039E7Q31150677-08B30093-EE33-41EA-8F99-AE231F58320DQ33639665-82FAC89F-FC24-4EC0-B936-70C52813FCC8Q33762051-02F2635A-9703-41D6-8A04-D51E3A7F720BQ33842617-80571BDC-43E0-46BC-87FF-BEFC5A2E4094Q34786984-DD208D26-2400-4D7A-86F7-A625F2BB113DQ36175896-B2272F06-F4BF-4952-852E-AACD021D0234Q36370999-3D497725-6C07-49F4-B8F9-34B6DDC1866CQ36639563-661CC299-5310-4B1D-B123-337F81CBCF00Q36791337-BD6D00B1-626B-442F-91D7-D15AF4B51F02Q36883672-3D50DB62-86C1-462E-9A27-B83BB4E5D8B2Q36922432-91E1B086-5880-41B0-9E87-7DA05E13E043Q36989630-FAEA898C-D5BD-46A5-B7EF-6CAB41C75A03Q37276243-0955265D-5BD0-44FB-8733-2AF2BA41BDFEQ37302360-E0496A7D-7195-4416-B259-A3BFC12682F8Q38270504-E97AA63A-9EA4-4985-B51F-F199A6A9A29FQ38599177-00107683-1064-46E9-8A73-456567290F0FQ39110484-83D44647-945A-4E8F-A19E-C1F957200501Q39111036-1D175890-50B0-4AC6-9E2C-ACFDB60D1EF8Q39226773-A51F89F6-21BC-4041-8971-F563B96B7FE2Q40293155-BE340363-7A7D-46B1-83D0-63018C149024Q41838943-3CF3EAFE-E8ED-410F-8F9B-4E32C84B5D0EQ42141044-2E4AEFFA-4FBD-49F5-BE4C-E79217EF5EC1Q42826580-ACE80F98-6C09-49BD-8C61-33B476D8FAFEQ43050672-071B1924-906F-48E2-96F3-DE9B22D1E0D7Q43215301-7962C57D-E824-4109-B616-1D5F5B85B345Q43738688-6F651141-600C-44C6-B14A-E7DD5E212959
P2860
A distinct meta-active conformation in the 1.1-A resolution structure of wild-type ApoCheY
description
2001 nî lūn-bûn
@nan
2001 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
A distinct meta-active conform ...... structure of wild-type ApoCheY
@ast
A distinct meta-active conform ...... structure of wild-type ApoCheY
@en
A distinct meta-active conform ...... structure of wild-type ApoCheY
@nl
type
label
A distinct meta-active conform ...... structure of wild-type ApoCheY
@ast
A distinct meta-active conform ...... structure of wild-type ApoCheY
@en
A distinct meta-active conform ...... structure of wild-type ApoCheY
@nl
prefLabel
A distinct meta-active conform ...... structure of wild-type ApoCheY
@ast
A distinct meta-active conform ...... structure of wild-type ApoCheY
@en
A distinct meta-active conform ...... structure of wild-type ApoCheY
@nl
P2860
P356
P1476
A distinct meta-active conform ...... structure of wild-type ApoCheY
@en
P2093
P2860
P304
P356
10.1074/JBC.C100295200
P407
P577
2001-08-03T00:00:00Z