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| | <StructureSection load='3fnq' size='340' side='right'caption='[[3fnq]], [[Resolution|resolution]] 1.85Å' scene=''> | | <StructureSection load='3fnq' size='340' side='right'caption='[[3fnq]], [[Resolution|resolution]] 1.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3fnq]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Blood_fluke Blood fluke]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FNQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FNQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3fnq]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Schistosoma_mansoni Schistosoma mansoni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FNQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FNQ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=HPA:HYPOXANTHINE'>HPA</scene>, <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]] 1.85Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3fb1|3fb1]], [[3faz|3faz]], [[1td1|1td1]], [[1tcv|1tcv]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=HPA:HYPOXANTHINE'>HPA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SmPNP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6183 Blood fluke])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Purine-nucleoside_phosphorylase Purine-nucleoside phosphorylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.1 2.4.2.1] </span></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=3fnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fnq OCA], [https://pdbe.org/3fnq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fnq RCSB], [https://www.ebi.ac.uk/pdbsum/3fnq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fnq ProSAT]</span></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=3fnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fnq OCA], [https://pdbe.org/3fnq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fnq RCSB], [https://www.ebi.ac.uk/pdbsum/3fnq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fnq ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/Q9BMI9_SCHMA Q9BMI9_SCHMA]] The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate (By similarity).[PIRNR:PIRNR000477]
| + | [https://www.uniprot.org/uniprot/Q9BMI9_SCHMA Q9BMI9_SCHMA] The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate (By similarity).[PIRNR:PIRNR000477] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Blood fluke]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Purine-nucleoside phosphorylase]] | + | [[Category: Schistosoma mansoni]] |
| - | [[Category: Castilho, M S]] | + | [[Category: Castilho MS]] |
| - | [[Category: Garratt, R C]] | + | [[Category: Garratt RC]] |
| - | [[Category: Oliva, G]] | + | [[Category: Oliva G]] |
| - | [[Category: Pereira, H M]] | + | [[Category: Pereira HM]] |
| - | [[Category: Glycosyltransferase]]
| + | |
| - | [[Category: Purine nucleoside phosphorylase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q9BMI9_SCHMA The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate (By similarity).[PIRNR:PIRNR000477]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Schistosomes are unable to synthesize purines de novo and depend exclusively on the salvage pathway for their purine requirements. It has been suggested that blockage of this pathway could lead to parasite death. The enzyme purine nucleoside phosphorylase (PNP) is one of its key components and molecules designed to inhibit the low-molecular-weight (LMW) PNPs, which include both the human and schistosome enzymes, are typically analogues of the natural substrates inosine and guanosine. Here, it is shown that adenosine both binds to Schistosoma mansoni PNP and behaves as a weak micromolar inhibitor of inosine phosphorolysis. Furthermore, the first crystal structures of complexes of an LMW PNP with adenosine and adenine are reported, together with those with inosine and hypoxanthine. These are used to propose a structural explanation for the selective binding of adenosine to some LMW PNPs but not to others. The results indicate that transition-state analogues based on adenosine or other 6-amino nucleosides should not be discounted as potential starting points for alternative inhibitors.
Adenosine binding to low-molecular-weight purine nucleoside phosphorylase: the structural basis for recognition based on its complex with the enzyme from Schistosoma mansoni.,Pereira HM, Rezende MM, Castilho MS, Oliva G, Garratt RC Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):73-9. Epub 2009 Dec, 21. PMID:20057051[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Pereira HM, Rezende MM, Castilho MS, Oliva G, Garratt RC. Adenosine binding to low-molecular-weight purine nucleoside phosphorylase: the structural basis for recognition based on its complex with the enzyme from Schistosoma mansoni. Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):73-9. Epub 2009 Dec, 21. PMID:20057051 doi:10.1107/S0907444909045715
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