Mechanism of transmembrane signaling by sensor histidine kinases

Author:

Gushchin Ivan12ORCID,Melnikov Igor3,Polovinkin Vitaly124,Ishchenko Andrii15,Yuzhakova Anastasia12ORCID,Buslaev Pavel2,Bourenkov Gleb6ORCID,Grudinin Sergei789ORCID,Round Ekaterina14,Balandin Taras1ORCID,Borshchevskiy Valentin12ORCID,Willbold Dieter110ORCID,Leonard Gordon3ORCID,Büldt Georg2,Popov Alexander3ORCID,Gordeliy Valentin124ORCID

Affiliation:

1. Institute of Complex Systems (ICS), ICS-6: Structural Biochemistry, Research Centre Jülich, 52425 Jülich, Germany.

2. Moscow Institute of Physics and Technology, 141700 Dolgoprudniy, Russia.

3. European Synchrotron Radiation Facility, F-38043 Grenoble, France.

4. Univ. Grenoble Alpes, CEA, CNRS, IBS, F-38000 Grenoble, France.

5. Institute of Crystallography, University of Aachen (RWTH), 52056 Aachen, Germany.

6. European Molecular Biology Laboratory, Hamburg Outstation, 22607 Hamburg, Germany.

7. Université Grenoble Alpes, LJK, F-38000 Grenoble, France.

8. CNRS, LJK, F-38000 Grenoble, France.

9. Inria, F-38000 Grenoble, France.

10. Institute of Physical Biology, Heinrich Heine University, 40225 Düsseldorf, Germany.

Abstract

Bacterial sensing mechanism revealed Escherichia coli use a transmembrane sensor protein to sense nitrate in their external environment and initiate a biochemical response. Gushchin et al. compared crystal structures of portions of the NarQ receptor that included the transmembrane helices in ligand-bound or unbound states. The structures suggest a signaling mechanism by which piston- and lever-like movements are transmitted to response regulator proteins within the cell. Such two-component systems are very common in bacteria and, if better understood, might provide targets for antimicrobial therapies. Science , this issue p. eaah6345

Funder

Ministry of Education and Science of the Russian Federation

FRISBI

GRAL

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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