1UN9

Crystal structure of the dihydroxyacetone kinase from C. freundii in complex with AMP-PNP and Mg2+

Summary for 1UN9

• Entry DOI: 10.2210/pdb1un9/pdb
• Related: 1UN8
• Descriptor: DIHYDROXYACETONE KINASE, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: kinase, glycerone kinase, dha kinase, dihydroxyacetone kinase
• Biological source: CITROBACTER FREUNDII
• Total number of polymer chains: 2
• Total formula weight: 116983.03

Authors

Siebold, C.,Arnold, I.,Garcia-Alles, L.F.,Baumann, U.,Erni, B. (deposition date: 2003-09-08, release date: 2003-10-30, Last modification date: 2025-10-01)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.1 Å)