A mechanism of covalent substrate binding in the x-ray structure of subunit K of the Escherichia coli dihydroxyacetone kinase - INSA Toulouse - Institut National des Sciences Appliquées de Toulouse
Article Dans Une Revue Proceedings of the National Academy of Sciences of the United States of America Année : 2003

A mechanism of covalent substrate binding in the x-ray structure of subunit K of the Escherichia coli dihydroxyacetone kinase

Christian Siebold
  • Fonction : Auteur
Bernhard Erni
  • Fonction : Auteur
Ulrich Baumann
  • Fonction : Auteur

Résumé

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.

Dates et versions

hal-03367160 , version 1 (06-10-2021)

Identifiants

Citer

Christian Siebold, Luis Fernando García-Alles, Bernhard Erni, Ulrich Baumann. A mechanism of covalent substrate binding in the x-ray structure of subunit K of the Escherichia coli dihydroxyacetone kinase. Proceedings of the National Academy of Sciences of the United States of America, 2003, 100 (14), pp.8188-8192. ⟨10.1073/pnas.0932787100⟩. ⟨hal-03367160⟩

Collections

INSA-TOULOUSE
18 Consultations
0 Téléchargements

Altmetric

Partager

More