(Q47754019)

5 February 2018

review article

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title

Mind your B's and R's: bacterial chemotaxis, signal transduction and protein recognition (English)

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5 February 2018

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Jurica MS

1

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5 February 2018

Stoddard BL

series ordinal

2

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5 February 2018

publication date

1 July 1998

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5 February 2018

published in

Structure

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5 February 2018

volume

6

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5 February 2018

issue

7

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5 February 2018

page(s)

809-813

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5 February 2018

Bacterial chemotaxis: a field in motion

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Crystal structure of the catalytic domain of the chemotaxis receptor methylesterase, CheB

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Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine

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

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Chemotaxis receptor recognition by protein methyltransferase CheR

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Communication modules in bacterial signaling proteins

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Signal transduction schemes of bacteria

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Bacterial chemotaxis and the molecular logic of intracellular signal transduction networks

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Roles of methylation and phosphorylation in the bacterial sensing system

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Protein methylation in behavioural control mechanisms and in signal transduction

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Structure of the Escherichia coli response regulator NarL

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The receptor binding site for the methyltransferase of bacterial chemotaxis is distinct from the sites of methylation

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The serine chemoreceptor from Escherichia coli is methylated through an inter-dimer process.

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Methylation of the Escherichia coli chemotaxis receptors: intra- and interdimer mechanisms

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Polar location of the chemoreceptor complex in the Escherichia coli cell.

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Receptor clustering as a cellular mechanism to control sensitivity

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High- and low-abundance chemoreceptors in Escherichia coli: differential activities associated with closely related cytoplasmic domains

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Global flexibility in a sensory receptor: a site-directed cross-linking approach.

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The cytoplasmic fragment of the aspartate receptor displays globally dynamic behavior.

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Structural basis for IL-4 receptor phosphopeptide recognition by the IRS-1 PTB domain

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DNA binding and cleavage by the nuclear intron-encoded homing endonuclease I-PpoI

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Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis

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Crystal structure of the dipeptide binding protein from Escherichia coli involved in active transport and chemotaxis

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7 January 2021

Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand

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7 January 2021

Refined structures of the ligand-binding domain of the aspartate receptor from Salmonella typhimurium.

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7 January 2021

Apo structure of the ligand-binding domain of aspartate receptor from Escherichia coli and its comparison with ligand-bound or pseudoligand-bound structures

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7 January 2021

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

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7 January 2021

Uncoupled phosphorylation and activation in bacterial chemotaxis. The 2.1-A structure of a threonine to isoleucine mutant at position 87 of CheY

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7 January 2021

Uncoupled phosphorylation and activation in bacterial chemotaxis. The 2.3 A structure of an aspartate to lysine mutant at position 13 of CheY

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7 January 2021

Structure and dynamics of a CheY-binding domain of the chemotaxis kinase CheA determined by nuclear magnetic resonance spectroscopy

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7 January 2021

NMR studies of the phosphotransfer domain of the histidine kinase CheA from Escherichia coli: assignments, secondary structure, general fold, and backbone dynamics

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7 January 2021

Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY

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7 January 2021

10.1016/S0969-2126(98)00082-3

Identifiers

DOI

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5 February 2018

1 reference

5 February 2018