Three-dimensional structural characterization of a novel Drosophila melanogaster acylphosphatase.
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.
Zuccotti
Simone
S
Department of Physics-INFM and Center of Excellence for Biomedical Research, University of Genova, Via Dodecaneso 33, 16132 Genova, Italy.
Rosano
Camillo
C
Ramazzotti
Matteo
M
Degl'Innocenti
Donatella
D
Stefani
Massimo
M
Manao
Giampaolo
G
Bolognesi
Martino
M
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
D017766:Acid Anhydride Hydrolases; D000097024:Acylphosphatase