PDBsum entry 1urr

Go to PDB code: 
protein ligands links
Hydrolase PDB id
Protein chain
97 a.a. *
Waters ×109
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: A novel drosophila melanogaster acylphosphatase (acpdro2)
Structure: Cg18505 protein. Chain: a. Synonym: acylphosphatase, acylphphtase, acyp2, cg18505. Engineered: yes
Source: Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Expressed in: escherichia coli. Expression_system_taxid: 562
1.50Å     R-factor:   0.163     R-free:   0.230
Authors: C.Rosano,S.Zuccotti,M.Bolognesi
Key ref:
S.Zuccotti et al. (2004). Three-dimensional structural characterization of a novel Drosophila melanogaster acylphosphatase. Acta Crystallogr D Biol Crystallogr, 60, 1177-1179. PubMed id: 15159593 DOI: 10.1107/S0907444904006808
03-Nov-03     Release date:   27-May-04    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q9VF36  (ACYP2_DROME) -  Acylphosphatase-2
102 a.a.
97 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Acylphosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: An acylphosphate + H2O = a carboxylate + phosphate
+ H(2)O
= carboxylate
+ phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     cellular metabolic process   1 term 
  Biochemical function     hydrolase activity     2 terms  


DOI no: 10.1107/S0907444904006808 Acta Crystallogr D Biol Crystallogr 60:1177-1179 (2004)
PubMed id: 15159593  
Three-dimensional structural characterization of a novel Drosophila melanogaster acylphosphatase.
S.Zuccotti, C.Rosano, M.Ramazzotti, D.Degl'Innocenti, M.Stefani, G.Manao, M.Bolognesi.
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.
  Selected figure(s)  
Figure 2.
A view into the proposed AcPDro2 phosphate-binding site. The active-site residue and the main-chain atoms of the P-loop (residues 19-24) are reported together with a residual electron-density peak (see text for details).
  The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2004, 60, 1177-1179) copyright 2004.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18451804 F.Bemporad, J.Gsponer, H.I.Hopearuoho, G.Plakoutsi, G.Stati, M.Stefani, N.Taddei, M.Vendruscolo, and F.Chiti (2008).
Biological function in a non-native partially folded state of a protein.
  EMBO J, 27, 1525-1535.  
16287076 A.Corazza, C.Rosano, K.Pagano, V.Alverdi, G.Esposito, C.Capanni, F.Bemporad, G.Plakoutsi, M.Stefani, F.Chiti, S.Zuccotti, M.Bolognesi, and P.Viglino (2006).
Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus.
  Proteins, 62, 64-79.
PDB codes: 1y9o 2bjd 2bje
16084386 C.Parrini, N.Taddei, M.Ramazzotti, D.Degl'Innocenti, G.Ramponi, C.M.Dobson, and F.Chiti (2005).
Glycine residues appear to be evolutionarily conserved for their ability to inhibit aggregation.
  Structure, 13, 1143-1151.  
16169977 G.Soldi, F.Bemporad, S.Torrassa, A.Relini, M.Ramazzotti, N.Taddei, and F.Chiti (2005).
Amyloid formation of a protein in the absence of initial unfolding and destabilization of the native state.
  Biophys J, 89, 4234-4244.  
16080154 K.Miyazono, Y.Sawano, and M.Tanokura (2005).
Crystal structure and structural stability of acylphosphatase from hyperthermophilic archaeon Pyrococcus horikoshii OT3.
  Proteins, 61, 196-205.  
  16508117 S.Zuccotti, C.Rosano, F.Bemporad, M.Stefani, and M.Bolognesi (2005).
Preliminary characterization of two different crystal forms of acylphosphatase from the hyperthermophile archaeon Sulfolobus solfataricus.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 61, 144-146.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.