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Title: Structure of 2-oxo-3-deoxygalactonate kinase from Klebsiella pneumoniae

Abstract

The crystal structure of 2-oxo-3-deoxygalactonate kinase from the De Ley–Doudoroff pathway of galactose metabolism has been determined at 2.1 Å resolution. In most organisms, efficient d-galactose utilization requires the highly conserved Leloir pathway that converts d-galactose to d-glucose 1-phosphate. However, in some bacterial and fungal species alternative routes of d-galactose assimilation have been identified. In the so-called De Ley–Doudoroff pathway, d-galactose is metabolized into pyruvate and d-glyceraldehyde 3-phosphate in five consecutive reactions carried out by specific enzymes. The penultimate step in this pathway involves the phosphorylation of 2-oxo-3-deoxygalactonate to 2-oxo-3-deoxygalactonate 6-phosphate catalyzed by 2-oxo-3-deoxygalactonate kinase, with ATP serving as a phosphoryl-group donor. Here, a crystal structure of 2-oxo-3-deoxygalactonate kinase from Klebsiella pneumoniae determined at 2.1 Å resolution is reported, the first structure of an enzyme from the De Ley–Doudoroff pathway. Structural comparison indicates that the enzyme belongs to the ASKHA (acetate and sugar kinases/hsc70/actin) family of phosphotransferases. The protein is composed of two α/β domains, each of which contains a core common to all family members. Additional elements introduced between conserved structural motifs define the unique features of 2-oxo-3-deoxygalactonate kinase and possibly determine the biological function of the protein.

Authors:
 [1];  [1]; ;  [1];  [1]
  1. Midwest Center for Structural Genomics, Biosciences Division, Argonne National Laboratory (United States)
Publication Date:
OSTI Identifier:
22351239
Resource Type:
Journal Article
Journal Name:
Acta Crystallographica. Section D: Biological Crystallography
Additional Journal Information:
Journal Volume: 67; Journal Issue: Pt 8; Other Information: PMCID: PMC3144851; PMID: 21795809; PUBLISHER-ID: dz5229; OAI: oai:pubmedcentral.nih.gov:3144851; Copyright (c) International Union of Crystallography 2011; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0907-4449
Country of Publication:
Denmark
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; ACETATES; CRYSTAL STRUCTURE; GLUCOSE; PHOSPHATES; RESOLUTION; SACCHAROSE

Citation Formats

Michalska, Karolina, Cuff, Marianne E., Structural Biology Center, Biosciences Division, Argonne National Laboratory, Tesar, Christine, Feldmann, Brian, Joachimiak, Andrzej, Structural Biology Center, Biosciences Division, Argonne National Laboratory, and Department of Biochemistry and Molecular Biology, University of Chicago. Structure of 2-oxo-3-deoxygalactonate kinase from Klebsiella pneumoniae. Denmark: N. p., 2011. Web. doi:10.1107/S0907444911021834.
Michalska, Karolina, Cuff, Marianne E., Structural Biology Center, Biosciences Division, Argonne National Laboratory, Tesar, Christine, Feldmann, Brian, Joachimiak, Andrzej, Structural Biology Center, Biosciences Division, Argonne National Laboratory, & Department of Biochemistry and Molecular Biology, University of Chicago. Structure of 2-oxo-3-deoxygalactonate kinase from Klebsiella pneumoniae. Denmark. https://doi.org/10.1107/S0907444911021834
Michalska, Karolina, Cuff, Marianne E., Structural Biology Center, Biosciences Division, Argonne National Laboratory, Tesar, Christine, Feldmann, Brian, Joachimiak, Andrzej, Structural Biology Center, Biosciences Division, Argonne National Laboratory, and Department of Biochemistry and Molecular Biology, University of Chicago. 2011. "Structure of 2-oxo-3-deoxygalactonate kinase from Klebsiella pneumoniae". Denmark. https://doi.org/10.1107/S0907444911021834.
@article{osti_22351239,
title = {Structure of 2-oxo-3-deoxygalactonate kinase from Klebsiella pneumoniae},
author = {Michalska, Karolina and Cuff, Marianne E. and Structural Biology Center, Biosciences Division, Argonne National Laboratory and Tesar, Christine and Feldmann, Brian and Joachimiak, Andrzej and Structural Biology Center, Biosciences Division, Argonne National Laboratory and Department of Biochemistry and Molecular Biology, University of Chicago},
abstractNote = {The crystal structure of 2-oxo-3-deoxygalactonate kinase from the De Ley–Doudoroff pathway of galactose metabolism has been determined at 2.1 Å resolution. In most organisms, efficient d-galactose utilization requires the highly conserved Leloir pathway that converts d-galactose to d-glucose 1-phosphate. However, in some bacterial and fungal species alternative routes of d-galactose assimilation have been identified. In the so-called De Ley–Doudoroff pathway, d-galactose is metabolized into pyruvate and d-glyceraldehyde 3-phosphate in five consecutive reactions carried out by specific enzymes. The penultimate step in this pathway involves the phosphorylation of 2-oxo-3-deoxygalactonate to 2-oxo-3-deoxygalactonate 6-phosphate catalyzed by 2-oxo-3-deoxygalactonate kinase, with ATP serving as a phosphoryl-group donor. Here, a crystal structure of 2-oxo-3-deoxygalactonate kinase from Klebsiella pneumoniae determined at 2.1 Å resolution is reported, the first structure of an enzyme from the De Ley–Doudoroff pathway. Structural comparison indicates that the enzyme belongs to the ASKHA (acetate and sugar kinases/hsc70/actin) family of phosphotransferases. The protein is composed of two α/β domains, each of which contains a core common to all family members. Additional elements introduced between conserved structural motifs define the unique features of 2-oxo-3-deoxygalactonate kinase and possibly determine the biological function of the protein.},
doi = {10.1107/S0907444911021834},
url = {https://www.osti.gov/biblio/22351239}, journal = {Acta Crystallographica. Section D: Biological Crystallography},
issn = {0907-4449},
number = Pt 8,
volume = 67,
place = {Denmark},
year = {Mon Aug 01 00:00:00 EDT 2011},
month = {Mon Aug 01 00:00:00 EDT 2011}
}