Structure of a transiently phosphorylated switch in bacterial signal transduction (Q27620864)

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Language	Label	Description	Also known as
English	Structure of a transiently phosphorylated switch in bacterial signal transduction	scientific article

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scholarly article

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Structure of a transiently phosphorylated switch in bacterial signal transduction (English)

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phosphorylation

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author name string

D Kern

1

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B F Volkman

2

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P Luginbühl

3

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M J Nohaile

4

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S Kustu

5

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D E Wemmer

6

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language of work or name

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publication date

December 1999

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402

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6764

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894-8

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Communication modules in bacterial signaling proteins

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https://api.crossref.org/works/10.1038%2F47273

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

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Structure of the Escherichia coli response regulator NarL

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based on heuristic

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

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

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

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Emergence of vancomycin tolerance in Streptococcus pneumoniae

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Structural and functional analyses of activating amino acid substitutions in the receiver domain of NtrC: evidence for an activating surface

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Phosphorylation of bacterial response regulator proteins by low molecular weight phospho-donors

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https://api.crossref.org/works/10.1038%2F47273

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Physical evidence for a phosphorylation-dependent conformational change in the enhancer-binding protein NtrC.

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https://api.crossref.org/works/10.1038%2F47273

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Structural conservation in the CheY superfamily

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Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis

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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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Millisecond-timescale motions contribute to the function of the bacterial response regulator protein Spo0F

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Structural basis of cyclin-dependent kinase activation by phosphorylation

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Activation mechanism of the MAP kinase ERK2 by dual phosphorylation

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Structural mechanism for glycogen phosphorylase control by phosphorylation and AMP

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A protein phosphorylation switch at the conserved allosteric site in GP

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Torsion angle dynamics for NMR structure calculation with the new program DYANA

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MOLMOL: a program for display and analysis of macromolecular structures

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