1un8

From Proteopedia

Revision as of 14:01, 30 October 2007

CRYSTAL STRUCTURE OF THE DIHYDROXYACETONE KINASE OF C. FREUNDII (NATIVE FORM)

Overview

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 Structure

1UN8 is a [Single protein] structure of sequence from [Citrobacter freundii] with MYY as [ligand]. Active as [Glycerone kinase], with EC number [2.7.1.29]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

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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