View source for 3k7y


==Aspartate Aminotransferase of Plasmodium falciparum==
<StructureSection load='3k7y' size='340' side='right'caption='[[3k7y]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3k7y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K7Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K7Y FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3k7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k7y OCA], [https://pdbe.org/3k7y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k7y RCSB], [https://www.ebi.ac.uk/pdbsum/3k7y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k7y ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O96142_PLAF7 O96142_PLAF7] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Aspartate aminotransferases (AspATs; EC 2.6.1.1) catalyze the conversion of aspartate and alpha-ketoglutarate into oxaloacetate and glutamate and are key enzymes in the nitrogen metabolism of all organisms. Recent findings suggest that the plasmodial enzyme [Plasmodium falciparum aspartate aminotransferase (PfAspAT)] may also play a pivotal role in energy metabolism and in the de novo biosynthesis of pyrimidines. However, while PfAspAT is a potential drug target, the high homology between the active sites of currently available AspAT structures hinders the development of specific inhibitors of these enzymes. In this article, we report the X-ray structure of the PfAspAT homodimer at a resolution of 2.8 A. While the overall fold is similar to the currently available structures of other AspATs, the structure presented shows a significant divergence in the conformation of the N-terminal residues. Deletion of these divergent PfAspAT N-terminal residues results in a loss of activity for the recombinant protein, and addition of a peptide containing these 13 N-terminal residues results in inhibition both in vitro and in a lysate isolated from cultured parasites, while the activity of human cytosolic AspAT is unaffected. The finding that the divergent N-terminal amino acids of PfAspAT play a role in catalytic activity indicates that specific inhibition of the enzyme may provide a lead for the development of novel compounds in the treatment of malaria. We also report on the localization of PfAspAT to the parasite cytosol and discuss the implications of the role of PfAspAT in the supply of malate to the parasite mitochondria.

Specific Inhibition of the Aspartate Aminotransferase of Plasmodium falciparum.,Wrenger C, Muller IB, Schifferdecker AJ, Jain R, Jordanova R, Groves MR J Mol Biol. 2011 Jan 28;405(4):956-71. Epub 2010 Nov 16. PMID:21087616<ref>PMID:21087616</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3k7y" style="background-color:#fffaf0;"></div>

==See Also==
*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Plasmodium falciparum 3D7]]
[[Category: Groves MR]]
[[Category: Jain R]]
[[Category: Jordanova R]]
[[Category: Muller IB]]
[[Category: Wrenger C]]