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Sensor histidine kinase NarQ activates via helical rotation, diagonal scissoring, and eventually piston-like shifts

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378271%3A_____%2F20%3A00563846" target="_blank" >RIV/68378271:_____/20:00563846 - isvavai.cz</a>

  • Result on the web

    <a href="https://hdl.handle.net/11104/0335635" target="_blank" >https://hdl.handle.net/11104/0335635</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3390/ijms21093110" target="_blank" >10.3390/ijms21093110</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Sensor histidine kinase NarQ activates via helical rotation, diagonal scissoring, and eventually piston-like shifts

  • Original language description

    Membrane-embedded sensor histidine kinases (HKs) and chemoreceptors are used ubiquitously by bacteria and archaea to percept the environment. Several mechanisms of transmembrane signal transduction in TCS receptors have been proposed, dubbed (swinging) piston, helical rotation, and diagonal scissoring. We extend our previous work on Escherichia coli nitrate/nitrite sensor kinase NarQ. We determined a crystallographic structure of the sensor-TM-HAMP fragment of the R50S mutant, which, unexpectedly, was found in a ligand-bound-like conformation, despite an inability to bind nitrate. Subsequently, we reanalyzed the structures of the ligand-free and ligand-bound NarQ and NarX sensor domains, and conducted extensive molecular dynamics simulations of ligand-free and ligand-bound wild type and mutated NarQ. Based on the data, we show that binding of nitrate to NarQ causes, first and foremost, helical rotation and diagonal scissoring of the α-helices at the core of the sensor domain.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10610 - Biophysics

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2020

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    International Journal of Molecular Sciences

  • ISSN

    1422-0067

  • e-ISSN

    1422-0067

  • Volume of the periodical

    21

  • Issue of the periodical within the volume

    9

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    18

  • Pages from-to

    3110

  • UT code for WoS article

    000535581700081

  • EID of the result in the Scopus database

    2-s2.0-85083968633