1un9: Difference between revisions

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.

1UN9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Citrobacter_freundii Citrobacter freundii] with MG, ANP and 2HA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glycerone_kinase Glycerone kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.29 2.7.1.29] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UN9 OCA].  

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