1a5c: Difference between revisions
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|ACTIVITY= [http://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13] </span> | ||
|GENE= | |GENE= | ||
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a5c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a5c OCA], [http://www.ebi.ac.uk/pdbsum/1a5c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a5c RCSB]</span> | |||
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[[Category: tim barrel]] | [[Category: tim barrel]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:33:33 2008'' | ||
Revision as of 18:33, 30 March 2008
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| , resolution 3.0Å | |||||||
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| Activity: | Fructose-bisphosphate aldolase, with EC number 4.1.2.13 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE FROM PLASMODIUM FALCIPARUM
OverviewOverview
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.
About this StructureAbout this Structure
1A5C is a Single protein structure of sequence from Plasmodium falciparum. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of fructose-1,6-bisphosphate aldolase from the human malaria parasite Plasmodium falciparum., Kim H, Certa U, Dobeli H, Jakob P, Hol WG, Biochemistry. 1998 Mar 31;37(13):4388-96. PMID:9521758
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