(Q27648812)

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The structure of a full-length response regulator from Mycobacterium tuberculosis in a stabilized three-dimensional domain-swapped, activated state

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scholarly article

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The structure of a full-length response regulator from Mycobacterium tuberculosis in a stabilized three-dimensional domain-swapped, activated state (English)

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Mycobacterium tuberculosis

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Efstratios Mylonas

object named as

Efstratios Mylonas

3

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Santosh Panjikar

object named as

Santosh Panjikar

4

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object named as

Dmitri I Svergun

6

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author name string

Jack King-Scott

1

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Elzbieta Nowak

2

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Manfred Roessle

5

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Paul A Tucker

7

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language of work or name

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publication date

28 December 2007

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Journal of Biological Chemistry

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282

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52

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37717-29

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Phosphoproteins involved in bacterial signal transduction.

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Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence

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A novel two-component system found in Mycobacterium tuberculosis

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Molecular characterization of the mycobacterial SenX3-RegX3 two-component system: evidence for autoregulation

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The senX3-regX3 two-component regulatory system of Mycobacterium tuberculosis is required for virulence

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The two-component regulatory system senX3-regX3 regulates phosphate-dependent gene expression in Mycobacterium smegmatis.

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From cell membrane to nucleotides: the phosphate regulon in Escherichia coli

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Gene regulation by phosphate in enteric bacteria

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The winged-helix DNA-binding motif: another helix-turn-helix takeoff

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Structural relationships in the OmpR family of winged-helix transcription factors

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Escherichia coli positive regulator OmpR has a large loop structure at the putative RNA polymerase interaction site

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Tandem Binding of Six OmpR Proteins to the ompF Upstream Regulatory Sequence of Escherichia coli

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

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Binding of the TorR regulator to cis-acting direct repeats activates tor operon expression

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Domain Orientation in the Inactive Response Regulator Mycobacterium tuberculosis MtrA Provides a Barrier to Activation † , ‡

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The structural basis of signal transduction for the response regulator PrrA from Mycobacterium tuberculosis

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

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

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Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain

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Evidence for phosphorylation-dependent conformational changes in methylesterase CheB.

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Multimerization of phosphorylated and non-phosphorylated ArcA is necessary for the response regulator function of the Arc two-component signal transduction system

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Molecular characterization of the PmrA regulon.

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Three-dimensional crystal structure of the transcription factor PhoB receiver domain

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Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active states

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3D domain swapping: as domains continue to swap

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Processing of X-ray diffraction data collected in oscillation mode

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Substructure solution with SHELXD

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Use of TLS parameters to model anisotropic displacements in macromolecular refinement

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Refinement of macromolecular structures by the maximum-likelihood method

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Main-chain bond lengths and bond angles in protein structures

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Histidine kinases and response regulator proteins in two-component signaling systems

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Domain swapping in the sporulation response regulator Spo0A

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Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface

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Three-dimensional solution structure of the N-terminal receiver domain of NTRC

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Crystal structure of the response regulator 02 receiver domain, the essential YycF two-component system of Streptococcus pneumoniae in both complexed and native states

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PRIMUS: a Windows PC-based system for small-angle scattering data analysis

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Observation of signal transduction in three-dimensional domain swapping

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Identifiers

10.1074/JBC.M705081200

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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