7cmj
From Proteopedia
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==Crystal structure of L.donovani Hypoxanthine-guanine phosphoribosyl transferase (HGPRT)== | ==Crystal structure of L.donovani Hypoxanthine-guanine phosphoribosyl transferase (HGPRT)== | ||
| - | <StructureSection load='7cmj' size='340' side='right'caption='[[7cmj]]' scene=''> | + | <StructureSection load='7cmj' size='340' side='right'caption='[[7cmj]], [[Resolution|resolution]] 2.76Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CMJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CMJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7cmj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_donovani_BPK282A1 Leishmania donovani BPK282A1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CMJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CMJ FirstGlance]. <br> |
| - | </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=7cmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cmj OCA], [https://pdbe.org/7cmj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cmj RCSB], [https://www.ebi.ac.uk/pdbsum/7cmj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cmj ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BA:BARIUM+ION'>BA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=7cmj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cmj OCA], [https://pdbe.org/7cmj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cmj RCSB], [https://www.ebi.ac.uk/pdbsum/7cmj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cmj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/E9BF84_LEIDB E9BF84_LEIDB] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Purine bases, synthesized de novo or recycled through the salvage pathway, are precursors of nucleotide synthesis and are essential in a variety of physiological processes including cell division, growth, signaling, energy metabolism and synthesis of vitamins/co-factor. The protozoan kinetoplastid parasites including Leishmania cannot synthesize de novo and rely solely on the purine salvage pathway, recycling the degraded products of nucleic acid metabolism. Enzymes of this pathway are thus of therapeutic importance. The enzyme Hypoxanthine-guanine phosphoribosyl transferase (HGPRT) (EC 2.4.2.8) plays a central role in this pathway, converting the purine base to its monophosphate product. Towards the elucidation of its role, we have cloned, expressed, purified and determined the crystal structure of L. donovani HGPRT at 2.76 A. Comparative structural analysis with the human homolog indicates differences in oligomer association. Comparative analyses identify insertions in the human homolog sequence in the tetramer interface. The results suggest that this difference can be exploited for therapeutic approaches. | ||
| + | |||
| + | The L.donovani Hypoxanthine-guanine phosphoribosyl transferase (HGPRT) oligomer is distinct from the human homolog.,Parihar PS, Pratap JV Biochem Biophys Res Commun. 2020 Nov 19;532(4):499-504. doi: , 10.1016/j.bbrc.2020.08.052. Epub 2020 Aug 30. PMID:32873391<ref>PMID:32873391</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7cmj" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Leishmania donovani BPK282A1]] | ||
[[Category: Parihar PS]] | [[Category: Parihar PS]] | ||
[[Category: Pratap JV]] | [[Category: Pratap JV]] | ||
Revision as of 10:32, 15 February 2023
Crystal structure of L.donovani Hypoxanthine-guanine phosphoribosyl transferase (HGPRT)
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