5JEQ

Fragment of nitrate/nitrite sensor histidine kinase NarQ (R50K) in symmetric apo state

5JEQ の概要

• エントリーDOI: 10.2210/pdb5jeq/pdb
• 関連するPDBエントリー: 5IJI 5JEF
• 分子名称: Nitrate/nitrite sensor protein NarQ, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: membrane protein, sensor, histidine kinase, nitrate, transferase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane ; Multi-pass membrane protein : P27896
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27354.72

構造登録者

Gushchin, I.,Melnikov, I.,Polovinkin, V.,Ishchenko, A.,Popov, A.,Gordeliy, V. (登録日: 2016-04-18, 公開日: 2017-05-31, 最終更新日: 2024-01-10)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.9 Å)