4FPP

Bacterial phosphotransferase

Summary for 4FPP

• Entry DOI: 10.2210/pdb4fpp/pdb
• Descriptor: phosphotransferase, NICKEL (II) ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: four helix bundle, bergerat fold, similar to type i histidine kinase, phosphotransferase, ccka, ctra, cpdr, bacterial cytoplasme, transferase
• Biological source: Caulobacter crescentus
• Total number of polymer chains: 3
• Total formula weight: 77814.07

Authors

Fioravanti, A.,Clantin, B.,Dewitte, F.,Lens, Z.,Verger, A.,Biondi, E.,Villeret, V. (deposition date: 2012-06-22, release date: 2012-09-12, Last modification date: 2024-02-28)

Primary citation

Fioravanti, A.,Clantin, B.,Dewitte, F.,Lens, Z.,Verger, A.,Biondi, E.G.,Villeret, V.
Structural insights into ChpT, an essential dimeric histidine phosphotransferase regulating the cell cycle in Caulobacter crescentus.
Acta Crystallogr.,Sect.F, 68:1025-1029, 2012

PubMed 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.

PubMed: 22949187
DOI: 10.1107/S1744309112033064

Experimental method

X-RAY DIFFRACTION (2.2 Å)