The structure at 2.4 A resolution of the protein from gene locus At3g21360, a putative Fe(II)/2-oxoglutarate-dependent enzyme from Arabidopsis thaliana

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 May 1;61(Pt 5):469-72. doi: 10.1107/S1744309105011565. Epub 2005 Apr 26.

Abstract

The crystal structure of the gene product of At3g21360 from Arabidopsis thaliana was determined by the single-wavelength anomalous dispersion method and refined to an R factor of 19.3% (Rfree = 24.1%) at 2.4 A resolution. The crystal structure includes two monomers in the asymmetric unit that differ in the conformation of a flexible domain that spans residues 178-230. The crystal structure confirmed that At3g21360 encodes a protein belonging to the clavaminate synthase-like superfamily of iron(II) and 2-oxoglutarate-dependent enzymes. The metal-binding site was defined and is similar to the iron(II) binding sites found in other members of the superfamily.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Arabidopsis / enzymology*
  • Arabidopsis / metabolism
  • Arabidopsis Proteins / chemistry*
  • Arabidopsis Proteins / metabolism
  • Binding Sites
  • Crystallization
  • Crystallography, X-Ray
  • Dual-Specificity Phosphatases
  • Iron / metabolism*
  • Ketoglutaric Acids / metabolism*
  • Mixed Function Oxygenases / chemistry
  • Mixed Function Oxygenases / metabolism
  • Models, Molecular
  • Protein Tyrosine Phosphatases / chemistry*
  • Protein Tyrosine Phosphatases / metabolism

Substances

  • Arabidopsis Proteins
  • Ketoglutaric Acids
  • Iron
  • Mixed Function Oxygenases
  • clavaminate synthase
  • DsPTP1 protein, Arabidopsis
  • Dual-Specificity Phosphatases
  • Protein Tyrosine Phosphatases

Associated data

  • PDB/1Y0Z
  • PDB/R1Y0ZSF