Three-dimensional structural characterization of a novel Drosophila melanogaster acylphosphatase

Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1177-9. doi: 10.1107/S0907444904006808. Epub 2004 May 21.

Abstract

Analysis of the Drosophila melanogaster EST database led to the discovery and cloning of a novel acylphosphatase. The CG18505 gene coding for a new enzyme (AcPDro2) is clearly distinct from the previously described CG16870Acyp gene, which also codes for a D. melanogaster acylphosphatase (AcPDro). The putative catalytic residues, together with residues held to stabilize the acylphosphatase fold, are conserved in the two encoded proteins. Crystals of AcPDro2, which belong to the trigonal space group P3(1)21, with unit-cell parameters a = b = 45.8, c = 98.6 angstroms, gamma = 120 degrees, allowed the solution of the protein structure by molecular replacement and its refinement to 1.5 angstroms resolution. The AcPDro2 active-site structure is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acid Anhydride Hydrolases / chemistry*
  • Acylphosphatase
  • Animals
  • Binding Sites
  • Catalysis
  • Catalytic Domain
  • Cloning, Molecular
  • Drosophila melanogaster / enzymology*
  • Expressed Sequence Tags
  • Humans
  • Models, Molecular
  • Protein Conformation
  • Protein Structure, Tertiary

Substances

  • Acid Anhydride Hydrolases