2J80

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

2J80 の概要

• エントリーDOI: 10.2210/pdb2j80/pdb
• 関連するPDBエントリー: 1P0Z 2J81
• 分子名称: SENSOR KINASE CITA, CITRATE ANION, SODIUM ION, ... (6 entities in total)
• 機能のキーワード: transferase, signal transduction, transmembrane, phosphorylation, two-component regulatory system
• 由来する生物種: KLEBSIELLA PNEUMONIAE
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30562.65

構造登録者

Sevvana, M.,Vijayan, V.,Zweckstetter, M.,Reinelt, S.,Madden, D.R.,Sheldrick, G.M.,Bott, M.,Griesinger, C.,Becker, S. (登録日: 2006-10-18, 公開日: 2007-10-23, 最終更新日: 2024-10-09)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.6 Å)