title: Structural insights into ChpT, an essential dimeric histidine phosphotransferase regulating the cell cycle in Caulobacter crescentus.
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.
authors.affiliation: Interdisciplinary 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.
authors.forename: Antonella
authors.initials: A
authors.lastname: Fioravanti
authors.forename: Bernard
authors.initials: B
authors.lastname: Clantin
authors.forename: Frédérique
authors.initials: F
authors.lastname: Dewitte
authors.forename: Zoé
authors.initials: Z
authors.lastname: Lens
authors.forename: Alexis
authors.initials: A
authors.lastname: Verger
authors.forename: Emanuele G
authors.initials: EG
authors.lastname: Biondi
authors.forename: Vincent
authors.initials: V
authors.lastname: Villeret
mesh_terms: D000595:Amino Acid Sequence; D016935:Caulobacter crescentus / Q000166:cytology / Q000201:enzymology*; D002453:Cell Cycle; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010770:Phosphotransferases / Q000737:chemistry*; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary
chemical_list: D010770:Phosphotransferases