Three-dimensional structural characterization of a novel Drosophila melanogaster acylphosphatase

被引：21
作者：
Zuccotti, S
Rosano, C
Ramazzotti, M
Degl'Innocenti, D
Stefani, M
Manao, G
Bolognesi, M
机构：
[1] Univ Genoa, INFM, Dept Phys, I-16132 Genoa, Italy
[2] Univ Genoa, Ctr Excellence Biomed Res, I-16132 Genoa, Italy
[3] Natl Inst Canc Res, Xray Struct Biol Unit, I-16132 Genoa, Italy
[4] Univ Florence, Dept Biochem Sci, I-50134 Florence, Italy
来源：
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2004年 / 60卷
关键词：
D O I：
10.1107/S0907444904006808
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
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 Angstrom, gamma=120degrees, allowed the solution of the protein structure by molecular replacement and its refinement to 1.5 Angstrom resolution. The AcPDro2 active-site structure is discussed.
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收藏
页码：1177 / 1179
页数：3
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