1A5C

FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE FROM PLASMODIUM FALCIPARUM

1A5C の概要

• エントリーDOI: 10.2210/pdb1a5c/pdb
• 分子名称: FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE (1 entity in total)
• 機能のキーワード: fructose-1, 6-bisphosphate aldolase, malaria, tim barrel, lyase
• 由来する生物種: Plasmodium falciparum (malaria parasite P. falciparum)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 80043.42

構造登録者

Kim, H.,Certa, U.,Dobeli, H.,Jakob, P.,Hol, W.G.J. (登録日: 1998-02-13, 公開日: 1998-06-10, 最終更新日: 2024-05-22)

主引用文献

Kim, H.,Certa, U.,Dobeli, H.,Jakob, P.,Hol, W.G.
Crystal structure of fructose-1,6-bisphosphate aldolase from the human malaria parasite Plasmodium falciparum.
Biochemistry, 37:4388-4396, 1998

PubMed Abstract: 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.

PubMed: 9521758
DOI: 10.1021/bi972233h

実験手法

X-RAY DIFFRACTION (3 Å)