View source for 6su1


==Trypanosoma congolense pyruvate kinase in complex with citrate and glycerol==
<StructureSection load='6su1' size='340' side='right'caption='[[6su1]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6su1]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_congolense_IL3000 Trypanosoma congolense IL3000]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SU1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SU1 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=6su1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6su1 OCA], [https://pdbe.org/6su1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6su1 RCSB], [https://www.ebi.ac.uk/pdbsum/6su1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6su1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G0UYF4_TRYCI G0UYF4_TRYCI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Trypanosoma are blood-borne parasites and are the causative agents of neglected tropical diseases (NTDs) affecting both humans and animals. These parasites mainly rely on glycolysis for their energy production within the mammalian host, which is why trypanosomal glycolytic enzymes have been pursued as interesting targets for the development of trypanocidal drugs. The structure-function relationships of pyruvate kinases (PYKs) from trypanosomatids (Trypanosoma and Leishmania) have been well-studied within this context. In this paper, we describe the structural and enzymatic characterization of PYK from T. congolense (TcoPYK), the main causative agent of Animal African Trypanosomosis (AAT), by employing a combination of enzymatic assays, thermal unfolding studies and X-ray crystallography.

Structural and kinetic characterization of Trypanosoma congolense pyruvate kinase.,Pinto Torres JE, Yuan M, Goossens J, Versees W, Caljon G, Michels PA, Walkinshaw MD, Magez S, Sterckx YG Mol Biochem Parasitol. 2020 Feb 19;236:111263. doi:, 10.1016/j.molbiopara.2020.111263. PMID:32084384<ref>PMID:32084384</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6su1" style="background-color:#fffaf0;"></div>

==See Also==
*[[Pyruvate kinase 3D structures|Pyruvate kinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Trypanosoma congolense IL3000]]
[[Category: Pinto Torres JE]]
[[Category: Sterckx YG-J]]