1un9: Difference between revisions
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Revision as of 17:01, 30 October 2007
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CRYSTAL STRUCTURE OF THE DIHYDROXYACETONE KINASE FROM C. FREUNDII IN COMPLEX WITH AMP-PNP AND MG2+
OverviewOverview
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. ... [(full description)]
About this StructureAbout this Structure
1UN9 is a [Single protein] structure of sequence from [Citrobacter freundii] with MG, ANP and 2HA as [ligands]. Active as [Glycerone kinase], with EC number [2.7.1.29]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of the Citrobacter freundii dihydroxyacetone kinase reveals an eight-stranded alpha-helical barrel ATP-binding domain., Siebold C, Arnold I, Garcia-Alles LF, Baumann U, Erni B, J Biol Chem. 2003 Nov 28;278(48):48236-44. Epub 2003 Sep 9. PMID:12966101
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