1UN8

Crystal structure of the dihydroxyacetone kinase of C. freundii (native form)

1UN8 の概要

• エントリーDOI: 10.2210/pdb1un8/pdb
• 関連するPDBエントリー: 1UN9
• 分子名称: DIHYDROXYACETONE KINASE, (2R)-3-(PHOSPHONOOXY)-2-(TETRADECANOYLOXY)PROPYL PALMITATE (3 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: CITROBACTER FREUNDII
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 117227.41

構造登録者

Siebold, C.,Arnold, I.,Garcia-Alles, L.F.,Baumann, U.,Erni, B. (登録日: 2003-09-08, 公開日: 2003-10-10, 最終更新日: 2024-05-08)

主引用文献

Siebold, C.,Arnold, I.,Garcia-Alles, L.F.,Baumann, U.,Erni, B.
Crystal Structure of the Citrobacter Freundii Dihydroxyacetone Kinase Reveals an Eight-Stranded Alpha-Helical Barrel ATP-Binding Domain
J.Biol.Chem., 278:48236-, 2003

PubMed Abstract: Dihydroxyacetone kinases are a sequence-conserved family of enzymes, which utilize two different phosphoryldonors, ATP in animals, plants and some bacteria, and a multiphosphoprotein of the phosphoenolpyruvate carbohydrate phosphotransferase system in bacteria. Here we report the 2.5-A crystal structure of the homodimeric Citrobacter freundii dihydroxyacetone kinase complex with an ATP analogue and dihydroxyacetone. The N-terminal domain consists of two alpha/beta-folds with a molecule of dihydroxyacetone covalently bound in hemiaminal linkage to the N epsilon 2 of His-220. The C-terminal domain consists of a regular eight-helix alpha-barrel. The eight helices form a deep pocket, which includes a tightly bound phospholipid. Only the lipid headgroup protrudes from the surface. The nucleotide is bound on the top of the barrel across from the entrance to the lipid pocket. The phosphate groups are coordinated by two Mg2+ ions to gamma-carboxyl groups of aspartyl residues. The ATP binding site does not contain positively charged or aromatic groups. Paralogues of dihydroxyacetone kinase also occur in association with transcription regulators and proteins of unknown function pointing to biological roles beyond triose metabolism.

PubMed: 12966101
DOI: 10.1074/JBC.M305942200

実験手法

X-RAY DIFFRACTION (2.5 Å)