1p9b: Difference between revisions
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==Structure of fully ligated Adenylosuccinate synthetase from Plasmodium falciparum== | ==Structure of fully ligated Adenylosuccinate synthetase from Plasmodium falciparum== | ||
<StructureSection load='1p9b' size='340' side='right' caption='[[1p9b]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1p9b' size='340' side='right'caption='[[1p9b]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1p9b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Plafa Plafa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P9B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P9B FirstGlance]. <br> | <table><tr><td colspan='2'>[[1p9b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Plafa Plafa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P9B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P9B FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1p9b" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1p9b" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Adenylosuccinate synthetase 3D structures|Adenylosuccinate synthetase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Adenylosuccinate synthase]] | [[Category: Adenylosuccinate synthase]] | ||
[[Category: Large Structures]] | |||
[[Category: Plafa]] | [[Category: Plafa]] | ||
[[Category: Anand, R P]] | [[Category: Anand, R P]] | ||
Revision as of 13:37, 27 November 2019
Structure of fully ligated Adenylosuccinate synthetase from Plasmodium falciparumStructure of fully ligated Adenylosuccinate synthetase from Plasmodium falciparum
Structural highlights
Function[PURA_PLAFA] Plays an important role in the salvage pathway for purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn 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. 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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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