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Acta Crystallogr Sect F Struct Biol Cryst Commun. Sep 1, 2012; 68(Pt 9): 1025–1029.
Published online Aug 29, 2012. doi:  10.1107/S1744309112033064
PMCID: PMC3433190
Structural insights into ChpT, an essential dimeric histidine phosphotransferase regulating the cell cycle in Caulobacter crescentus
Antonella Fioravanti,a Bernard Clantin,a Frédérique Dewitte,a Zoé Lens,a Alexis Verger,a Emanuele G. Biondi,a and Vincent Villereta*
aInterdisciplinary Research Institute, USR 3078 CNRS – Université Lille Nord de France, Parc CNRS de la Haute Borne, 50 Avenue de Halley, 59658 Villeneuve d’Ascq, France
Correspondence e-mail: vincent.villeret/at/iri.univ-lille1.fr
Received June 23, 2012; Accepted July 20, 2012.
Abstract
Two-component and phosphorelay signal-transduction proteins are crucial for bacterial cell-cycle regulation in Caulobacter crescentus. ChpT is an essential histidine phosphotransferase that controls the activity of the master cell-cycle regulator CtrA by phosphorylation. Here, the 2.2 Å resolution crystal structure of ChpT is reported. ChpT is a homodimer and adopts the domain architecture of the intracellular part of class I histidine kinases. Each subunit consists of two distinct domains: an N-terminal helical hairpin domain and a C-terminal α/β domain. The two N-terminal domains are adjacent within the dimer, forming a four-helix bundle. The ChpT C-terminal domain adopts an atypical Bergerat ATP-binding fold.
Keywords: bacterial cell cycle, Caulobacter crescentus, histidine kinases, histidine phosphotransferases
Articles from Acta Crystallographica Section F: Structural Biology and Crystallization Communications are provided here courtesy of
International Union of Crystallography