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Three-dimensional structural characterization of a novel Drosophila melanogaster acylphosphatase

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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 P3121, with unit-cell parameters a = b = 45.8, c = 98.6 Å,  = 120°, allowed the solution of the protein structure by molecular replacement and its refinement to 1.5 Å resolution. The AcPDro2 active-site structure is discussed.

Keywords: Drosophila melanogaster; acylphosphatase

Document Type: Short Communication

DOI: http://dx.doi.org/10.1107/S0907444904006808

Publication date: June 1, 2004

bsc/ayd/2004/00000060/00000006/art00037
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