Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Three-dimensional structural characterization of a novel Drosophila melanogaster acylphosphatase.,Zuccotti S, Rosano C, Ramazzotti M, Degl'Innocenti D, Stefani M, Manao G, Bolognesi M Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1177-9. Epub 2004, May 21. PMID:15159593[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zuccotti S, Rosano C, Ramazzotti M, Degl'Innocenti D, Stefani M, Manao G, Bolognesi M. Three-dimensional structural characterization of a novel Drosophila melanogaster acylphosphatase. Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1177-9. Epub 2004, May 21. PMID:15159593 doi:10.1107/S0907444904006808
