1OI3

X-ray structure of the dihydroxyacetone kinase from Escherichia coli

Summary for 1OI3

• Entry DOI: 10.2210/pdb1oi3/pdb
• Related: 1OI2
• Descriptor: HYPOTHETICAL PROTEIN YCGT, SULFATE ION (3 entities in total)
• Functional Keywords: kinase, dihydroxyacetone kinase, ycgt
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 2
• Total formula weight: 79257.34

Authors

Siebold, C.,Garcia-Alles, L.-F.,Erni, B.,Baumann, U. (deposition date: 2003-06-04, release date: 2003-07-14, Last modification date: 2024-05-08)

Primary citation

Siebold, C.,Garcia-Alles, L.-F.,Erni, B.,Baumann, U.
A Mechanism of Covalent Substrate Binding in the X-Ray Structure of Subunit K of the Escherichia Coli Dihydroxyacetone Kinase
Proc.Natl.Acad.Sci.USA, 100:8188-, 2003

PubMed Abstract: 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.

PubMed: 12813127
DOI: 10.1073/PNAS.0932787100

Experimental method

X-RAY DIFFRACTION (2 Å)