4FPP

Bacterial phosphotransferase

4FPP の概要

• エントリーDOI: 10.2210/pdb4fpp/pdb
• 分子名称: phosphotransferase, NICKEL (II) ION, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: four helix bundle, bergerat fold, similar to type i histidine kinase, phosphotransferase, ccka, ctra, cpdr, bacterial cytoplasme, transferase
• 由来する生物種: Caulobacter crescentus
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 77814.07

構造登録者

Fioravanti, A.,Clantin, B.,Dewitte, F.,Lens, Z.,Verger, A.,Biondi, E.,Villeret, V. (登録日: 2012-06-22, 公開日: 2012-09-12, 最終更新日: 2024-02-28)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.2 Å)