4fym: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[4fym]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FYM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FYM FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4fym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fym OCA], [https://pdbe.org/4fym PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fym RCSB], [https://www.ebi.ac.uk/pdbsum/4fym PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fym ProSAT]</span></td></tr>
 </table>
 == Function ==
 [https://www.uniprot.org/uniprot/Q8N0R1_PLAFA Q8N0R1_PLAFA]
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The most severe form of malaria is caused by the obligate parasite Plasmodium falciparum. Orotate phosphoribosyltransferase (OPRTase) is the fifth enzyme in the de novo pyrimidine-synthesis pathway in the parasite, which lacks salvage pathways. Among all of the malaria de novo pyrimidine-biosynthesis enzymes, the structure of P. falciparum OPRTase (PfOPRTase) was the only one unavailable until now. PfOPRTase that could be crystallized was obtained after some low-complexity sequences were removed. Four catalytic dimers were seen in the asymmetic unit (a total of eight polypeptides). In addition to revealing unique amino acids in the PfOPRTase active sites, asymmetric dimers in the larger structure pointed to novel parasite-specific protein-protein interactions that occlude the catalytic active sites. The latter could potentially modulate PfOPRTase activity in parasites and possibly provide new insights for blocking PfOPRTase functions.
-Structure of Plasmodium falciparum orotate phosphoribosyltransferase with autologous inhibitory protein-protein interactions.,Kumar S, Krishnamoorthy K, Mudeppa DG, Rathod PK Acta Crystallogr F Struct Biol Commun. 2015 May;71(Pt 5):600-8. doi:, 10.1107/S2053230X1500549X. Epub 2015 Apr 21. PMID:25945715<ref>PMID:25945715</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4fym" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>