1p9b: Difference between revisions

Revision as of 12:54, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1p9b.png

Template:STRUCTURE 1p9b

Structure of fully ligated Adenylosuccinate synthetase from Plasmodium falciparumStructure of fully ligated Adenylosuccinate synthetase from Plasmodium falciparum

Template:ABSTRACT PUBMED 14729341

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

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OCA

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-'''Structure of fully ligated Adenylosuccinate synthetase from Plasmodium falciparum'''
+===Structure of fully ligated Adenylosuccinate synthetase from Plasmodium falciparum===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_14729341}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14729341 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_14729341}}
 ==About this Structure==
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 [[Category: Sumathy, K.]]
 [[Category: Ligase]]
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