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Science. 2017 Jun 9;356(6342). pii: eaah6345. doi: 10.1126/science.aah6345. Epub 2017 May 18.

Mechanism of transmembrane signaling by sensor histidine kinases.

Author information

1
Institute of Complex Systems (ICS), ICS-6: Structural Biochemistry, Research Centre Jülich, 52425 Jülich, Germany. ivan.gushchin@phystech.edu valentin.gordeliy@ibs.fr.
2
Moscow Institute of Physics and Technology, 141700 Dolgoprudniy, Russia.
3
European Synchrotron Radiation Facility, F-38043 Grenoble, France.
4
Institute of Complex Systems (ICS), ICS-6: Structural Biochemistry, Research Centre Jülich, 52425 Jülich, Germany.
5
Univ. Grenoble Alpes, CEA, CNRS, IBS, F-38000 Grenoble, France.
6
Institute of Crystallography, University of Aachen (RWTH), 52056 Aachen, Germany.
7
European Molecular Biology Laboratory, Hamburg Outstation, 22607 Hamburg, Germany.
8
Université Grenoble Alpes, LJK, F-38000 Grenoble, France.
9
CNRS, LJK, F-38000 Grenoble, France.
10
Inria, F-38000 Grenoble, France.
11
Institute of Physical Biology, Heinrich Heine University, 40225 Düsseldorf, Germany.

Abstract

One of the major and essential classes of transmembrane (TM) receptors, present in all domains of life, is sensor histidine kinases, parts of two-component signaling systems (TCSs). The structural mechanisms of TM signaling by these sensors are poorly understood. We present crystal structures of the periplasmic sensor domain, the TM domain, and the cytoplasmic HAMP domain of the Escherichia coli nitrate/nitrite sensor histidine kinase NarQ in the ligand-bound and mutated ligand-free states. The structures reveal that the ligand binding induces rearrangements and pistonlike shifts of TM helices. The HAMP domain protomers undergo leverlike motions and convert these pistonlike motions into helical rotations. Our findings provide the structural framework for complete understanding of TM TCS signaling and for development of antimicrobial treatments targeting TCSs.

PMID:
28522691
DOI:
10.1126/science.aah6345
[Indexed for MEDLINE]

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