1p9b: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:1p9b.gif|left|200px]] | [[Image:1p9b.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1p9b", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
| | --> | ||
| | {{STRUCTURE_1p9b| PDB=1p9b | SCENE= }} | ||
}} | |||
'''Structure of fully ligated Adenylosuccinate synthetase from Plasmodium falciparum''' | '''Structure of fully ligated Adenylosuccinate synthetase from Plasmodium falciparum''' | ||
Line 33: | Line 30: | ||
[[Category: Murthy, M R.]] | [[Category: Murthy, M R.]] | ||
[[Category: Sumathy, K.]] | [[Category: Sumathy, K.]] | ||
[[Category: | [[Category: Ligase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:50:43 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on |
Revision as of 04:50, 3 May 2008
Structure of fully ligated Adenylosuccinate synthetase from Plasmodium falciparum
OverviewOverview
In the absence of the de novo purine nucleotide biosynthetic pathway in parasitic protozoa, purine salvage is of primary importance for parasite survival. Enzymes of the salvage pathway are, therefore, good targets for anti-parasitic drugs. Adenylosuccinate synthetase (AdSS), catalysing the first committed step in the synthesis of AMP from IMP, is a potential target for anti-protozoal chemotherapy. We report here the crystal structure of adenylosuccinate synthetase from the malaria parasite, Plasmodium falciparum, complexed to 6-phosphoryl IMP, GDP, Mg2+ and the aspartate analogue, hadacidin at 2 A resolution. The overall architecture of P. falciparum AdSS (PfAdSS) is similar to the known structures from Escherichia coli, mouse and plants. Differences in substrate interactions seen in this structure provide a plausible explanation for the kinetic differences between PfAdSS and the enzyme from other species. Additional hydrogen bonding interactions of the protein with GDP may account for the ordered binding of substrates to the enzyme. The dimer interface of PfAdSS is also different, with a pronounced excess of positively charged residues. Differences highlighted here provide a basis for the design of species-specific inhibitors of the enzyme.
About this StructureAbout this Structure
1P9B is a Single protein structure of sequence from Plasmodium falciparum. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of fully ligated adenylosuccinate synthetase from Plasmodium falciparum., Eaazhisai K, Jayalakshmi R, Gayathri P, Anand RP, Sumathy K, Balaram H, Murthy MR, J Mol Biol. 2004 Jan 30;335(5):1251-64. PMID:14729341 Page seeded by OCA on Sat May 3 04:50:43 2008