TY  - JOUR
AU  - Gushchin, Ivan
AU  - Melnikov, Igor
AU  - Polovinkin, Vitaly
AU  - Ishchenko, Andrii
AU  - Yuzhakova, Anastasia
AU  - Buslaev, Pavel
AU  - Bourenkov, Gleb
AU  - Grudinin, Sergei
AU  - Round, Ekaterina
AU  - Balandin, Taras
AU  - Borshchevskiy, Valentin
AU  - Willbold, Dieter
AU  - Leonard, Gordon
AU  - Büldt, Georg
AU  - Popov, Alexander
AU  - Gordeliy, Valentin
TI  - Mechanism of transmembrane signaling by sensor histidine kinases
JO  - Science
VL  - 356
IS  - 6342
SN  - 0036-8075
CY  - Washington, DC [u.a.]
PB  - American Association for the Advancement of Science
M1  - FZJ-2017-04108
SP  - 6345
PY  - 2017
AB  - One of the major and essential classes of transmembrane (TM) receptors, present in all domains of life, is sensor histidine kinases (HKs), parts of two-component signaling systems (TCS). The structural mechanisms of transmembrane signaling by these sensors are poorly understood. We present here crystal structures of the periplasmic sensor domain, the TM domain and the cytoplasmic HAMP domain of the Escherichia coli nitrate/nitrite sensor HK NarQ in the ligand-bound and mutated ligand-free states. The structures reveal that the ligand binding induces significant rearrangements and piston-like shifts of TM helices. The HAMP domain protomers undergo lever-like motions and convert the piston-like motions into helical rotations. Our findings provide the structural framework for complete understanding of TM TCS signaling and for development of antimicrobial treatments targeting TCS.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000402871700044
C6  - pmid:28522691
DO  - DOI:10.1126/science.aah6345
UR  - https://juser.fz-juelich.de/record/834107
ER  -