2PC4 Lyase date Mar 29, 2007
title Crystal Structure Of Fructose-Bisphosphate Aldolase From Plasmodium Falciparum In Complex With Trap-Tail Determined At 2.4 Angstrom Resolution
authors J.Bosch, C.A.Buscaglia, B.Krumm, T.Cardozo, V.Nussenzweig, W.G.J.Hol, Structural Genomics Of Pathogenic Protozoa Consortium (Sgpp)
compound source
Molecule: Fructose-Bisphosphate Aldolase
Chain: A, B, C, D
Synonym: 41 Kda Antigen
Ec: 4.1.2.13
Engineered: Yes
Organism_scientific: Plasmodium Falciparum
Organism_common: Malaria Parasite
Expression_system: Escherichia Coli
Expression_system_common: Bacteria
Expression_system_strain: Bl21star(De3)
Expression_system_vector_type: Plasmid
Expression_system_vector: T7 System
Expression_system_plasmid: Pet14b

Molecule: Pbtrap
Chain: H
Fragment: C-Terminus: Residues 601-606
Engineered: Yes

Synthetic: Yes
Other_details: Synthetic Peptide With The Sequence Based On Pbtrap Protein From Plasmodium Berghei, Unp Entry P90573, P90573_plabe, Residues 601-606
symmetry Space Group: P 21 21 21
R_factor 0.198
crystal
cell
length a length b length c angle alpha angle beta angle gamma
70.386 145.519 148.520 90.00 90.00 90.00
method X-Ray Diffractionresolution 2.40 Å
ligand
enzyme Lyase E.C.4.1.2.13 BRENDA
Gene PBTRAP (P. berghei)
Gene
Ontology
ChainFunctionProcessComponent
A, D, C
  • catalytic activity
  • fructose-bisphosphate aldola...
  • lyase activity
  • glycolysis
  • metabolic process

  • Primary referenceAldolase provides an unusual binding site for thrombospondin-related anonymous protein in the invasion machinery of the malaria parasite., Bosch J, Buscaglia CA, Krumm B, Ingason BP, Lucas R, Roach C, Cardozo T, Nussenzweig V, Hol WG, Proc Natl Acad Sci U S A. 2007 Apr 24;104(17):7015-20. Epub 2007 Apr 10. PMID:17426153
    Data retrieval
  • Asymmetric unit, PDB entry: [header only] [complete with coordinates] (239 Kb) [Save to disk]
  • Biological Unit Coordinates (2pc4.pdb1.gz) 227 Kb
  • CSU: Contacts of Structural Units for 2PC4
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