5IJI

Fragment of nitrate/nitrite sensor histidine kinase NarQ (WT) in symmetric holo state

Summary for 5IJI

• Entry DOI: 10.2210/pdb5iji/pdb
• Descriptor: Nitrate/nitrite sensor histidine kinase NarQ, EICOSANE, NITRATE ION, ... (4 entities in total)
• Functional Keywords: membrane protein, sensor, histidine kinase, nitrate, transferase
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane ; Multi-pass membrane protein : P27896
• Total number of polymer chains: 1
• Total formula weight: 28287.64

Authors

Gushchin, I.,Melnikov, I.,Polovinkin, V.,Ishchenko, A.,Popov, A.,Gordeliy, V. (deposition date: 2016-03-02, release date: 2017-05-31, Last modification date: 2024-05-08)

Primary citation

Gushchin, I.,Melnikov, I.,Polovinkin, V.,Ishchenko, A.,Yuzhakova, A.,Buslaev, P.,Bourenkov, G.,Grudinin, S.,Round, E.,Balandin, T.,Borshchevskiy, V.,Willbold, D.,Leonard, G.,Buldt, G.,Popov, A.,Gordeliy, V.
Mechanism of transmembrane signaling by sensor histidine kinases.
Science, 356:-, 2017

PubMed 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 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.

PubMed: 28522691
DOI: 10.1126/science.aah6345

Experimental method

X-RAY DIFFRACTION (1.94 Å)