(Q27627158)

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A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in signal transduction

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10997904%20AND%20SRC:MED&resulttype=core&format=json

10 November 2019

A transient interaction between two phosphorelay proteins trapped in a crystal lattice reveals the mechanism of molecular recognition and phosphotransfer in signal transduction (English)

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10997904%20AND%20SRC:MED&resulttype=core&format=json

10 November 2019

phosphorelay signal transduction system

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2

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10 November 2019

author name string

J Zapf

1

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10 November 2019

Madhusudan

3

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10 November 2019

J A Hoch

4

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10 November 2019

K I Varughese

5

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10 November 2019

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1 August 2000

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10 November 2019

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10 November 2019

8

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10 November 2019

8

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10 November 2019

851-862

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10 November 2019

Initiation of sporulation in B. subtilis is controlled by a multicomponent phosphorelay

1 reference

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Protein aspartate phosphatases control the output of two-component signal transduction systems

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Deactivation of the sporulation transcription factor Spo0A by the Spo0E protein phosphatase

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Yeast HOG1 MAP kinase cascade is regulated by a multistep phosphorelay mechanism in the SLN1-YPD1-SSK1 "two-component" osmosensor.

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Phosphorelay signal transduction: the emerging family of plant response regulators

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Three-dimensional structure of CheY, the response regulator of bacterial chemotaxis

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Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis

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Structure of the Escherichia coli response regulator NarL

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7 January 2021

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High-resolution NMR structure and backbone dynamics of the Bacillus subtilis response regulator, Spo0F: implications for phosphorylation and molecular recognition

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7 January 2021

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

1 reference

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7 January 2021

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

1 reference

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7 January 2021

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Conformational changes induced by phosphorylation of the FixJ receiver domain

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Phosphorylated aspartate in the structure of a response regulator protein

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7 January 2021

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Structure of a transiently phosphorylated switch in bacterial signal transduction

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Formation of a novel four-helix bundle and molecular recognition sites by dimerization of a response regulator phosphotransferase

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Solution structure of the homodimeric core domain of Escherichia coli histidine kinase EnvZ

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7 January 2021

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

1 reference

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7 January 2021

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Molecular recognition in signal transduction: the interaction surfaces of the Spo0F response regulator with its cognate phosphorelay proteins revealed by alanine scanning mutagenesis

1 reference

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7 January 2021

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Two-component signal transduction in Bacillus subtilis: how one organism sees its world.

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The change in hydrogen bond strength accompanying charge rearrangement: implications for enzymatic catalysis

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7 January 2021

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A phosphotransferase activity of the Bacillus subtilis sporulation protein Spo0F that employs phosphoramidate substrates.

1 reference

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7 January 2021

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Enzyme-Catalyzed Phosphoryl Transfer Reactions

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Divalent metal ion binding to the CheY protein and its significance to phosphotransfer in bacterial chemotaxis

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A source of response regulator autophosphatase activity: the critical role of a residue adjacent to the Spo0F autophosphorylation active site

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Insights into eukaryotic multistep phosphorelay signal transduction revealed by the crystal structure of Ypd1p from Saccharomyces cerevisiae

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Transcriptional regulation of the Enterococcus faecium BM4147 vancomycin resistance gene cluster by the VanS-VanR two-component regulatory system in Escherichia coli K-12.

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Alanine mutants of the Spo0F response regulator modifying specificity for sensor kinases in sporulation initiation

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Identifiers

10.1016/S0969-2126(00)00174-X

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10997904%20AND%20SRC:MED&resulttype=core&format=json

10 November 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10997904%20AND%20SRC:MED&resulttype=core&format=json

10 November 2019

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