1oi2
From Proteopedia
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X-RAY STRUCTURE OF THE DIHYDROXYACETONE KINASE FROM ESCHERICHIA COLI
Overview
Dihydroxyacetone (Dha) kinases are homologous proteins that use different, phosphoryl donors, a multiphosphoryl protein of the, phosphoenolpyruvate-dependent carbohydrate:phosphotransferase system in, bacteria, ATP in animals, plants, and some bacteria. The Dha kinase of, Escherichia coli consists of three subunits, DhaK and DhaL, which are, colinear to the ATP-dependent Dha kinases of eukaryotes, and the, multiphosphoryl protein DhaM. Here we show the crystal structure of the, DhaK subunit in complex with Dha at 1.75 A resolution. DhaK is a homodimer, with a fold consisting of two six-stranded mixed beta-sheets surrounded by, nine alpha-helices and a beta-ribbon covering the exposed edge strand of, one sheet. The core of the N-terminal domain has an alpha/beta fold common, to subunits of carbohydrate transporters and transcription regulators of, the phosphoenolpyruvate-dependent carbohydrate:phosphotransferase system., The core of the C-terminal domain has a fold similar to the C-terminal, domain of the cell-division protein FtsZ. A molecule of Dha is covalently, bound in hemiaminal linkage to the N epsilon 2 of His-230. The hemiaminal, does not participate in covalent catalysis but is the chemical basis for, discrimination between short-chain carbonyl compounds and polyols., Paralogs of Dha kinases occur in association with transcription regulators, of the TetR/QacR and the SorC families, pointing to their biological role, as sensors in signaling.
About this Structure
1OI2 is a Single protein structure of sequence from Escherichia coli with SO4 and GOL as ligands. Active as Glycerone kinase, with EC number 2.7.1.29 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
A mechanism of covalent substrate binding in the x-ray structure of subunit K of the Escherichia coli dihydroxyacetone kinase., Siebold C, Garcia-Alles LF, Erni B, Baumann U, Proc Natl Acad Sci U S A. 2003 Jul 8;100(14):8188-92. Epub 2003 Jun 17. PMID:12813127
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