2V9A

Structure of Citrate-free Periplasmic Domain of Sensor Histidine Kinase CitA

Summary for 2V9A

• Entry DOI: 10.2210/pdb2v9a/pdb
• Related: 1P0Z 2J80
• Descriptor: SENSOR KINASE CITA (2 entities in total)
• Functional Keywords: signal transduction, sensor histidine kinase, cita, kinase, membrane, transferase, sensor domain, transmembrane, inner membrane, phosphorylation, two-component regulatory system
• Biological source: KLEBSIELLA PNEUMONIAE
• Total number of polymer chains: 2
• Total formula weight: 28998.88

Authors

Sevvana, M.,Vijayan, V.,Zweckstetter, M.,Reinelt, S.,Madden, D.R.,Sheldrick, G.M.,Bott, M.,Griesinger, C.,Becker, S. (deposition date: 2007-08-23, release date: 2008-03-25, Last modification date: 2023-12-13)

Primary citation

Sevvana, M.,Vijayan, V.,Zweckstetter, M.,Reinelt, S.,Madden, D.R.,Herbst-Irmer, R.,Sheldrick, G.M.,Bott, M.,Griesinger, C.,Becker, S.
A Ligand-Induced Switch in the Periplasmic Domain of Sensor Histidine Kinase Cita.
J.Mol.Biol., 377:512-, 2008

PubMed Abstract: 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.

PubMed: 18258261
DOI: 10.1016/J.JMB.2008.01.024

Experimental method

X-RAY DIFFRACTION (2 Å)