Quaternary structure of human, Drosophila melanogaster and Caenorhabditis elegans MFE-2 in solution from synchrotron small-angle X-ray scattering

FEBS Lett. 2013 Feb 14;587(4):305-10. doi: 10.1016/j.febslet.2012.12.014. Epub 2013 Jan 8.

Abstract

Multifunctional enzyme type 2 (MFE-2) forms part of the fatty acid β-oxidation pathway in peroxisomes. MFE-2s from various species reveal proteins with structurally homologous functional domains assembled in different compilations. Crystal structures of all domain types are known. SAXS data from human, fruit fly and Caenorhabditiselegans MFE-2s and their constituent domains were collected, and both ab initio and rigid body models constructed. Location of the putative substrate binding helper domain SCP-2L (sterol carrier protein 2-like), which is not part of MFE-2 protein in every species and not seen as part of any previous MFE-2 structures, was determined. The obtained models of human and C. elegans MFE-2 lend a direct structural support to the idea of the biological role of SCP-2L.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 17-Hydroxysteroid Dehydrogenases / chemistry*
  • 17-Hydroxysteroid Dehydrogenases / genetics
  • 17-Hydroxysteroid Dehydrogenases / metabolism
  • 3-Hydroxyacyl CoA Dehydrogenases / chemistry*
  • 3-Hydroxyacyl CoA Dehydrogenases / genetics
  • 3-Hydroxyacyl CoA Dehydrogenases / metabolism
  • Alcohol Oxidoreductases / chemistry*
  • Alcohol Oxidoreductases / genetics
  • Alcohol Oxidoreductases / metabolism
  • Animals
  • Caenorhabditis elegans / enzymology
  • Caenorhabditis elegans Proteins / chemistry*
  • Caenorhabditis elegans Proteins / genetics
  • Caenorhabditis elegans Proteins / metabolism
  • Carbon-Oxygen Lyases / chemistry*
  • Carbon-Oxygen Lyases / genetics
  • Carbon-Oxygen Lyases / metabolism
  • Carrier Proteins / chemistry
  • Dimerization
  • Drosophila Proteins / chemistry*
  • Drosophila Proteins / genetics
  • Drosophila Proteins / metabolism
  • Drosophila melanogaster / enzymology
  • Enoyl-CoA Hydratase / chemistry*
  • Enoyl-CoA Hydratase / genetics
  • Enoyl-CoA Hydratase / metabolism
  • Humans
  • Hydro-Lyases / chemistry*
  • Hydro-Lyases / genetics
  • Hydro-Lyases / metabolism
  • Models, Molecular*
  • Multienzyme Complexes / chemistry*
  • Multienzyme Complexes / genetics
  • Multienzyme Complexes / metabolism
  • Peptide Fragments / chemistry
  • Peptide Fragments / genetics
  • Peptide Fragments / metabolism
  • Peroxisomal Multifunctional Protein-2
  • Peroxisomes / enzymology
  • Protein Structure, Tertiary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Scattering, Small Angle
  • Solubility
  • Species Specificity
  • Synchrotrons
  • X-Ray Diffraction

Substances

  • Caenorhabditis elegans Proteins
  • Carrier Proteins
  • Drosophila Proteins
  • MFE-2 protein, C elegans
  • Mfe2 protein, Drosophila
  • Multienzyme Complexes
  • Peptide Fragments
  • Recombinant Proteins
  • sterol carrier proteins
  • 17-Hydroxysteroid Dehydrogenases
  • Alcohol Oxidoreductases
  • 3-Hydroxyacyl CoA Dehydrogenases
  • Carbon-Oxygen Lyases
  • Hydro-Lyases
  • Peroxisomal Multifunctional Protein-2
  • HSD17B4 protein, human
  • Enoyl-CoA Hydratase