A common dimerization interface in bacterial response regulators KdpE and TorR. - Wikidata - awgldk - TriplyDB

A common dimerization interface in bacterial response regulators KdpE and TorR.

A common dimerization interface in bacterial response regulators KdpE and TorR.

http://www.wikidata.org/entity/Q36476585

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Prokaryotic 2-component systems and the OmpR/PhoB superfamily The aspartate-less receiver (ALR) domains: distribution, structure and function Domain Orientation in the Inactive Response Regulator Mycobacterium tuberculosis MtrA Provides a Barrier to Activation † , ‡Crystal Structures of the Receiver Domain of the Response Regulator PhoP from Escherichia coli in the Absence and Presence of the Phosphoryl Analog Beryllofluoride The structure of a full-length response regulator from Mycobacterium tuberculosis in a stabilized three-dimensional domain-swapped, activated state Structure of the DNA-Binding Domain of the Response Regulator PhoP from Mycobacterium tuberculosis † , ‡Crystal Structure of a Complex between the Phosphorelay Protein YPD1 and the Response Regulator Domain of SLN1 Bound to a Phosphoryl Analog Determinants for the Activation and Autoinhibition of the Diguanylate Cyclase Response Regulator WspR Regulation of Response Regulator Autophosphorylation through Interdomain Contacts Structure of the Response Regulator PhoP from Mycobacterium tuberculosis Reveals a Dimer through the Receiver Domain The Atypical Response Regulator Protein ChxR Has Structural Characteristics and Dimer Interface Interactions That Are Unique within the OmpR/PhoB Subfamily Structure-Function Studies of DNA Binding Domain of Response Regulator KdpE Reveals Equal Affinity Interactions at DNA Half-Sites The dimeric form of the unphosphorylated response regulator BaeR An asymmetric heterodomain interface stabilizes a response regulator–DNA complex Atypical Response Regulator ChxR from Chlamydia trachomatis Is Structurally Poised for DNA Binding Structural dynamics of the two-component response regulator RstA in recognition of promoter DNA element The structural basis of signal transduction for the response regulator PrrA from Mycobacterium tuberculosis The Arabidopsis B-type response regulator 18 homomerizes and positively regulates cytokinin responses.Comprehensive analysis of OmpR phosphorylation, dimerization, and DNA binding supports a canonical model for activation.Identification of sensory and signal-transducing domains in two-component signaling systems.Evolution of two-component signal transduction systems Interactions of the CpxA sensor kinase and cognate CpxR response regulator from Yersinia pseudotuberculosis.Activation of the diguanylate cyclase PleD by phosphorylation-mediated dimerization.DNA consensus sequence motif for binding response regulator PhoP, a virulence regulator of Mycobacterium tuberculosis.Identification of OmpR-family response regulators interacting with thioredoxin in the Cyanobacterium Synechocystis sp. PCC 6803.Conformational Dynamics of Response Regulator RegX3 from Mycobacterium tuberculosis.Structure of the Response Regulator NsrR from Streptococcus agalactiae, Which Is Involved in Lantibiotic Resistance.The Two-Component System ChtRS Contributes to Chlorhexidine Tolerance in Enterococcus faecium Intramolecular arrangement of sensor and regulator overcomes relaxed specificity in hybrid two-component systems.Statistical analyses of protein sequence alignments identify structures and mechanisms in signal activation of sensor histidine kinases Bacterial response regulators: versatile regulatory strategies from common domains.Structural basis of DNA sequence recognition by the response regulator PhoP in Mycobacterium tuberculosis 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.The Response Regulator BfmR Is a Potential Drug Target for Acinetobacter baumannii.System-level mapping of Escherichia coli response regulator dimerization with FRET hybrids.Probing 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 dynamics Molecular strategies for phosphorylation-mediated regulation of response regulator activity.Crystal structure of the inactive state of the receiver domain of Spo0A from Paenisporosarcina sp. TG-14, a psychrophilic bacterium isolated from an Antarctic glacier.A new perspective on response regulator activation.

P2860

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P2860

A common dimerization interface in bacterial response regulators KdpE and TorR.

http://www.wikidata.org/entity/Q36476585

description

2005 nî lūn-bûn

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2005年の論文

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年學術文章

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2005年學術文章

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2005年學術文章

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name

A common dimerization interface in bacterial response regulators KdpE and TorR.

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A common dimerization interface in bacterial response regulators KdpE and TorR.

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type

label

A common dimerization interface in bacterial response regulators KdpE and TorR.

@ast

A common dimerization interface in bacterial response regulators KdpE and TorR.

@en

prefLabel

A common dimerization interface in bacterial response regulators KdpE and TorR.

@ast

A common dimerization interface in bacterial response regulators KdpE and TorR.

@en

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Protein Science

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A common dimerization interface in bacterial response regulators KdpE and TorR.

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Alejandro Toro-Roman

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Ti Wu

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P2860

The Protein Data Bank

BeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate: structure of a BeF(3)(-) complex with phosphoserine phosphatase

KdpD and KdpE, proteins that control expression of the kdpABC operon, are members of the two-component sensor-effector class of regulators

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Evidence of intradomain and interdomain flexibility in an OmpR/PhoB homolog from Thermotoga maritima

Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator

Domain arrangement of Der, a switch protein containing two GTPase domains

Structural Analysis of the Domain Interface in DrrB, a Response Regulator of the OmpR/PhoB Subfamily

A response regulatory protein with the site of phosphorylation blocked by an arginine interaction: crystal structure of Spo0F from Bacillus subtilis

Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD): a vehicle for direct determination of three-dimensional structure

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3077-3088

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10.1110/PS.051722805

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12

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14

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2005-12-01T00:00:00Z

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2253231

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