1a5c
From Proteopedia
(New page: 200px<br /><applet load="1a5c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a5c, resolution 3.0Å" /> '''FRUCTOSE-1,6-BISPHOSP...) |
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| - | [[Image:1a5c.gif|left|200px]]<br /><applet load="1a5c" size=" | + | [[Image:1a5c.gif|left|200px]]<br /><applet load="1a5c" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1a5c, resolution 3.0Å" /> | caption="1a5c, resolution 3.0Å" /> | ||
'''FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE FROM PLASMODIUM FALCIPARUM'''<br /> | '''FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE FROM PLASMODIUM FALCIPARUM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the glycolytic enzyme class I fructose-1, 6-bisphosphate | + | 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 Structure== | ==About this Structure== | ||
| - | 1A5C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Active as [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] Full crystallographic information is available from [http:// | + | 1A5C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A5C OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Certa, U.]] | [[Category: Certa, U.]] | ||
[[Category: Dobeli, H.]] | [[Category: Dobeli, H.]] | ||
| - | [[Category: Hol, W | + | [[Category: Hol, W G.J.]] |
[[Category: Jakob, P.]] | [[Category: Jakob, P.]] | ||
[[Category: Kim, H.]] | [[Category: Kim, H.]] | ||
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[[Category: tim barrel]] | [[Category: tim barrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:41:01 2008'' |
Revision as of 09:41, 21 February 2008
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FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE FROM PLASMODIUM FALCIPARUM
Overview
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 Structure
1A5C is a Single protein structure of sequence from Plasmodium falciparum. Active as Fructose-bisphosphate aldolase, with EC number 4.1.2.13 Full crystallographic information is available from OCA.
Reference
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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