Insights into multistep phosphorelay from the crystal structure of the C-terminal HPt domain of ArcB (Q27734899)

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T Mizuno

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T Shimizu

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T Hakoshima

Hyphal development in Neurospora crassa: involvement of a two-component histidine kinase

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language of work or name

English

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publication date

7 March 1997

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published in

Cell

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volume

88

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page(s)

717-23

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issue

5

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cites work

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Signal transduction via the multi-step phosphorelay: not necessarily a road less traveled

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Structure of the Escherichia coli response regulator NarL

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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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SKN7, a yeast multicopy suppressor of a mutation affecting cell wall beta-glucan assembly, encodes a product with domains homologous to prokaryotic two-component regulators and to heat shock transcription factors

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

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Arabidopsis ethylene-response gene ETR1: similarity of product to two-component regulators

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Cation-promoted association of a regulatory and target protein is controlled by protein phosphorylation

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1H, 15N, and 13C backbone chemical shift assignments, secondary structure, and magnesium-binding characteristics of the Bacillus subtilis response regulator, Spo0F, determined by heteronuclear high-resolution NMR.

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Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1

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Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0-A resolution

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Protein structure comparison by alignment of distance matrices

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Ethylene insensitivity conferred by Arabidopsis ERS gene

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Active-centre torsion-angle strain revealed in 1.6 Å-resolution structure of histidine-containing phosphocarrier protein

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Improved methods for building protein models in electron density maps and the location of errors in these models

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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PROCHECK: a program to check the stereochemical quality of protein structures

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

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A novel sensor-regulator protein that belongs to the homologous family of signal-transduction proteins involved in adaptive responses in Escherichia coli.

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A yeast protein similar to bacterial two-component regulators

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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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Improved Fourier coefficients for maps using phases from partial structures with errors

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

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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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Histidine and aspartate phosphorylation: two-component systems and the limits of homology

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Phosphotransfer circuitry of the putative multi-signal transducer, ArcB, of Escherichia coli: in vitro studies with mutants

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Integration of multiple domains in a two-component sensor protein: the Bordetella pertussis BvgAS phosphorelay

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

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Crystal structure of Myxococcus xanthus nucleoside diphosphate kinase and its interaction with a nucleotide substrate at 2.0 A resolution

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Three-dimensional structure of the Escherichia coli phosphocarrier protein IIIglc

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