TY  - JOUR
AU  - Gushchin, Ivan
AU  - Melnikov, Igor
AU  - Polovinkin, Vitaly
AU  - Ishchenko, Andrii
AU  - Gordeliy, Valentin
TI  - Crystal Structure of a Proteolytic Fragment of the Sensor Histidine Kinase NarQ
JO  - Crystals
VL  - 10
IS  - 3
SN  - 2073-4352
CY  - Basel
PB  - MDPI
M1  - FZJ-2020-01642
SP  - 149 -
PY  - 2020
AB  - Two-component signaling systems (TCSs) are a large and important class of sensory systems in bacteria, archaea, and some eukaryotes, yet their mechanism of action is still not fully understood from the structural point of view. Many TCS receptors are elongated flexible proteins with transmembrane (TM) regions, and are difficult to work with. Consequently, truncated fragments of the receptors are often used in structural studies. However, it is not fully clear whether the structures of the fragments correspond well to their native structures in the context of full-length proteins. Recently, we crystallized a fragment of Escherichia coli nitrate/nitrite sensor histidine kinase, NarQ, encompassing the sensor, TM, and HAMP domains. Here we report that a smaller proteolytic fragment consisting of the sensor and TM domains can also be crystallized using the in meso approach. The structure of the fragment is similar to the previously determined one, with minor differences in the vicinity of the truncation site. The results show that the crystallization of such sensor–TM fragments can be accomplished and can provide information on the packing of transmembrane helices, albeit limited, and that the proteolysis may or may not be a problem during crystallization.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000523512100051
DO  - DOI:10.3390/cryst10030149
UR  - https://juser.fz-juelich.de/record/874733
ER  -