Open AccessStructural insights into ChpT, an essential dimeric histidine phosphotransferase regulating the cell cycle in Caulobacter crescentus
Author(s) -
Fioravanti Antonella,
Clantin Bernard,
Dewitte Frédérique,
Lens Zoé,
Verger Alexis,
Biondi Emanuele G.,
Villeret Vincent
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112033064
Subject(s) - caulobacter crescentus , histidine kinase , microbiology and biotechnology , biology , pep group translocation , response regulator , phosphorylation , histidine , dimer , intracellular , phosphotransferase , cell cycle , kinase , protein subunit , signal transduction , hamp domain , biochemistry , chemistry , cell , binding domain , binding site , enzyme , bacterial protein , gene , organic chemistry , phosphoenolpyruvate carboxykinase
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.