title: Three-dimensional structural characterization of a novel Drosophila melanogaster acylphosphatase.
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.
authors.affiliation: Department of Physics-INFM and Center of Excellence for Biomedical Research, University of Genova, Via Dodecaneso 33, 16132 Genova, Italy.
authors.forename: Simone
authors.initials: S
authors.lastname: Zuccotti
authors.forename: Camillo
authors.initials: C
authors.lastname: Rosano
authors.forename: Matteo
authors.initials: M
authors.lastname: Ramazzotti
authors.forename: Donatella
authors.initials: D
authors.lastname: Degl'Innocenti
authors.forename: Massimo
authors.initials: M
authors.lastname: Stefani
authors.forename: Giampaolo
authors.initials: G
authors.lastname: Manao
authors.forename: Martino
authors.initials: M
authors.lastname: Bolognesi
mesh_terms: D017766:Acid Anhydride Hydrolases / Q000737:chemistry*; D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D020134:Catalytic Domain; D003001:Cloning, Molecular; D004331:Drosophila melanogaster / Q000201:enzymology*; D020224:Expressed Sequence Tags; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D000097024:Acylphosphatase
chemical_list: D017766:Acid Anhydride Hydrolases; D000097024:Acylphosphatase