3EZI

Crystal Structure of the E. coli Histidine Kinase NarX Sensor Domain without Ligand

Summary for 3EZI

• Entry DOI: 10.2210/pdb3ezi/pdb
• Related: 3EZH
• Descriptor: Nitrate/nitrite sensor protein narX, ISOPROPYL ALCOHOL (3 entities in total)
• Functional Keywords: histidine kinase sensor domain, cell inner membrane, cell membrane, kinase, membrane, nitrate assimilation, phosphoprotein, transferase, transmembrane, two-component regulatory system
• Biological source: Escherichia coli K12
• Cellular location: Cell inner membrane ; Multi-pass membrane protein : P0AFA2
• Total number of polymer chains: 4
• Total formula weight: 47810.00

Authors

Cheung, J.,Hendrickson, W.A. (deposition date: 2008-10-22, release date: 2008-12-23, Last modification date: 2023-12-27)

Primary citation

Cheung, J.,Hendrickson, W.A.
Structural Analysis of Ligand Stimulation of the Histidine Kinase NarX.
Structure, 17:190-201, 2009

PubMed Abstract: Histidine kinase receptors are a large family of membrane-spanning proteins found in many prokaryotes and some eukaryotes. They are a part of two-component signal transduction systems, which each comprise a sensor kinase and a response regulator and are involved with the regulation of many cellular processes. NarX is a histidine kinase receptor that responds to nitrate and nitrite to effect regulation of anaerobic respiration in various bacteria. We present high-resolution X-ray crystal structures of the periplasmic sensor domain from Escherichia coli NarX in a complex with nitrate and in the apo state. Our analysis reveals that nitrate-binding induces conformation changes that result in a piston-type displacement between the N- and C-terminal helices of the periplasmic domain. Such conformational changes might represent a conserved mechanism of signaling in histidine kinases by which ligand binding is communicated across the lipid bilayer.

PubMed: 19217390
DOI: 10.1016/j.str.2008.12.013

Experimental method

X-RAY DIFFRACTION (1.7 Å)