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Updated: May 18, 2026

Synchronization of Caulobacter Crescentus for Investigation of the Bacterial Cell Cycle
Published on: April 8, 2015
Structural insights into ChpT, an essential dimeric histidine phosphotransferase regulating the cell cycle in
Antonella Fioravanti1, Bernard Clantin, Frédérique Dewitte
1Interdisciplinary 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.
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.
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