View source for 6rn1


==Structure of N-terminal truncated Plasmodium falciparum IMP-nucleotidase==
<StructureSection load='6rn1' size='340' side='right'caption='[[6rn1]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6rn1]] is a 2 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=6RN1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RN1 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]] 3&#8491;</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=6rn1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rn1 OCA], [https://pdbe.org/6rn1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rn1 RCSB], [https://www.ebi.ac.uk/pdbsum/6rn1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rn1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ISN1_PLAF7 ISN1_PLAF7] Specifically, catalyzes the dephosphorylation of inosine monophosphate (IMP) into inosine (PubMed:32591529). By dephosphorylating IMP, plays a role in the purine salvage pathway (PubMed:32591529). Does not have phosphotransferase activity with IMP as phosphate donor and adenosine as phosphate acceptor (PubMed:32591529).<ref>PMID:32591529</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Plasmodium falciparum (Pf) relies solely on the salvage pathway for its purine nucleotide requirements, making this pathway indispensable to the parasite. Purine nucleotide levels are regulated by anabolic processes and by nucleotidases that hydrolyse these metabolites into nucleosides. Certain apicomplexan parasites, including Pf, have an IMP-specific-nucleotidase 1 (ISN1). Here we show, by comprehensive substrate screening, that PfISN1 catalyzes the dephosphorylation of inosine monophosphate (IMP) and is allosterically activated by ATP. Crystal structures of tetrameric PfISN1 reveal complex rearrangements of domain organization tightly associated with catalysis. Immunofluorescence microscopy and expression of GFP-fused protein indicate cytosolic localization of PfISN1 and expression in asexual and gametocyte stages of the parasite. With earlier evidence on isn1 upregulation in female gametocytes, the structures reported in this study may contribute to initiate the design for possible transmission-blocking agents.

Structure and catalytic regulation of Plasmodium falciparum IMP specific nucleotidase.,Carrique L, Ballut L, Shukla A, Varma N, Ravi R, Violot S, Srinivasan B, Ganeshappa UT, Kulkarni S, Balaram H, Aghajari N Nat Commun. 2020 Jun 26;11(1):3228. doi: 10.1038/s41467-020-17013-x. PMID:32591529<ref>PMID:32591529</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6rn1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Plasmodium falciparum 3D7]]
[[Category: Aghajari N]]
[[Category: Ballut L]]
[[Category: Carrique L]]
[[Category: Violot S]]