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PDBsum entry 1a5c
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of fructose-1,6-Bisphosphate aldolase from the human malaria parasite plasmodium falciparum.
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Authors
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H.Kim,
U.Certa,
H.Döbeli,
P.Jakob,
W.G.Hol.
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Ref.
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Biochemistry, 1998,
37,
4388-4396.
[DOI no: ]
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PubMed id
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Abstract
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The structure of the glycolytic enzyme class I fructose-1, 6-bisphosphate
aldolase from the human malaria parasite Plasmodium falciparum has been
determined by X-ray crystallography. Homotetrameric P. falciparum aldolase
(PfALDO) crystallizes in space group P3221 with one 80 kDa dimer per asymmetric
unit. The final refined PfALDO model has an R-factor of 0.239 and an R-free of
0.329 with respect to data from 8 to 3.0 A resolution. PfALDO is potentially a
target for antimalarial drug design as the intraerythrocytic merozoite lifestage
of P. falciparum is completely dependent upon glycolysis for its ATP production.
Thus, inhibitors directed against the glycolytic enzymes in P. falciparum may be
effective in killing the parasite. The structure of PfALDO is compared with the
previously determined structure of human aldolase in order to determine possible
targets for the structure-based design of selective PfALDO ligands. The salient
structural differences include a hydrophobic pocket on the surface of PfALDO,
which results from some amino acid changes and a single residue deletion
compared with human aldolase, and the overall quaternary structure of the PfALDO
tetramer, which buries less surface area than human aldolase.
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