Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 68, Issue -, Pages 1025-1029Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309112033064
Keywords
bacterial cell cycle; Caulobacter crescentus; histidine kinases; histidine phosphotransferases
Funding
- CNRS (Centre National de la Recherche Scientifique, CNRS/USTL, France)
- ANR [ANR_11_SVJ3_003_01]
- Region Nord Pas-de-Calais
- CPER CIA
- University of Lille Nord de France
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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 angstrom 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 alpha/beta 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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