Journal
STRUCTURE
Volume 17, Issue 2, Pages 190-201Publisher
CELL PRESS
DOI: 10.1016/j.str.2008.12.013
Keywords
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Funding
- Howard Hughes Medical Institute Funding Source: Medline
- NIGMS NIH HHS [R01 GM034102-24, R01 GM034102, R01 GM034102-21, R01 GM034102-22, R01 GM034102-23, GM34102, R37 GM034102] Funding Source: Medline
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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 histicline kinases by which ligand binding is communicated across the lipid bilayer.
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