2v9a
From Proteopedia
STRUCTURE OF CITRATE-FREE PERIPLASMIC DOMAIN OF SENSOR HISTIDINE KINASE CITA
Overview
Sensor histidine kinases of two-component signal-transduction systems are essential for bacteria to adapt to variable environmental conditions. However, despite their prevalence, it is not well understood how extracellular signals such as ligand binding regulate the activity of these sensor kinases. CitA is the sensor histidine kinase in Klebsiella pneumoniae that regulates the transport and anaerobic metabolism of citrate in response to its extracellular concentration. We report here the X-ray structures of the periplasmic sensor domain of CitA in the citrate-free and citrate-bound states. A comparison of the two structures shows that ligand binding causes a considerable contraction of the sensor domain. This contraction may represent the molecular switch that activates transmembrane signaling in the receptor.
About this Structure
2V9A is a Single protein structure of sequence from Klebsiella pneumoniae. Full crystallographic information is available from OCA.
Reference
A ligand-induced switch in the periplasmic domain of sensor histidine kinase CitA., Sevvana M, Vijayan V, Zweckstetter M, Reinelt S, Madden DR, Herbst-Irmer R, Sheldrick GM, Bott M, Griesinger C, Becker S, J Mol Biol. 2008 Mar 21;377(2):512-23. Epub 2008 Jan 16. PMID:18258261 Page seeded by OCA on Sun May 4 18:24:52 2008
Categories: Histidine kinase | Klebsiella pneumoniae | Single protein | Becker, S. | Bott, M. | Griesinger, C. | Madden, D R. | Reinelt, S. | Sevvana, M. | Sheldrick, G M. | Vijayan, V. | Zweckstetter, M. | Cita | Inner membrane | Kinase | Membrane | Phosphorylation | Sensor domain | Sensor histidine kinase | Signal transduction | Transferase | Transmembrane | Two-component regulatory system
