2btd

From Proteopedia

Revision as of 12:18, 30 October 2007

CRYSTAL STRUCTURE OF DHAL FROM E. COLI

Overview

Dihydroxyacetone (Dha) kinases are a family of sequence-related enzymes, that utilize either ATP or phosphoenolpyruvate (PEP) as source of high, energy phosphate. The PEP-dependent Dha kinase of Escherichia coli, consists of three subunits. DhaK and DhaL are homologous to the Dha and, nucleotide-binding domains of the ATP-dependent kinase of Citrobacter, freundii. The DhaM subunit is a multiphosphorylprotein of the PEP:sugar, phosphotransferase system (PTS). DhaL contains a tightly bound ADP as, coenzyme that gets transiently phosphorylated in the double displacement, of phosphate between DhaM and Dha. Here we report the 2.6A crystal, structure of the E.coli DhaL subunit. DhaL folds into an eight-helix, barrel of regular up-down topology with a hydrophobic core made up of, eight ... [(full description)]

About this Structure

2BTD is a [Single protein] structure of sequence from [Escherichia coli] with MG and ADP as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Crystal structure of the nucleotide-binding subunit DhaL of the Escherichia coli dihydroxyacetone kinase., Oberholzer AE, Schneider P, Baumann U, Erni B, J Mol Biol. 2006 Jun 9;359(3):539-45. Epub 2006 Apr 18. PMID:16647083

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