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| | <StructureSection load='2xox' size='340' side='right'caption='[[2xox]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='2xox' size='340' side='right'caption='[[2xox]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2xox]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Leido Leido]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XOX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2XOX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2xox]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_donovani Leishmania donovani]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XOX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XOX 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]] 2.5Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pteridine_reductase Pteridine reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.33 1.5.1.33] </span></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'>[http://proteopedia.org/fgij/fg.htm?mol=2xox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xox OCA], [http://pdbe.org/2xox PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xox RCSB], [http://www.ebi.ac.uk/pdbsum/2xox PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xox 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=2xox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xox OCA], [https://pdbe.org/2xox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xox RCSB], [https://www.ebi.ac.uk/pdbsum/2xox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xox ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q6QDB5_LEIDO Q6QDB5_LEIDO] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Leido]] | + | [[Category: Leishmania donovani]] |
| - | [[Category: Pteridine reductase]]
| + | [[Category: Barrack KL]] |
| - | [[Category: Barrack, K L]] | + | [[Category: Burke LA]] |
| - | [[Category: Burke, L A]] | + | [[Category: Fyfe PK]] |
| - | [[Category: Fyfe, P K]] | + | [[Category: Hunter WN]] |
| - | [[Category: Hunter, W N]] | + | [[Category: Tulloch LB]] |
| - | [[Category: Tulloch, L B]] | + | |
| - | [[Category: Antifolate]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Short-chain reductase]]
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| Structural highlights
Function
Q6QDB5_LEIDO
Publication Abstract from PubMed
Pteridine reductase (PTR1) is a potential target for drug development against parasitic Trypanosoma and Leishmania species, protozoa that are responsible for a range of serious diseases found in tropical and subtropical parts of the world. As part of a structure-based approach to inhibitor development, specifically targeting Leishmania species, well ordered crystals of L. donovani PTR1 were sought to support the characterization of complexes formed with inhibitors. An efficient system for recombinant protein production was prepared and the enzyme was purified and crystallized in an orthorhombic form with ammonium sulfate as the precipitant. Diffraction data were measured to 2.5 A resolution and the structure was solved by molecular replacement. However, a sulfate occupies a phosphate-binding site used by NADPH and occludes cofactor binding. The nicotinamide moiety is a critical component of the active site and without it this part of the structure is disordered. The crystal form obtained under these conditions is therefore unsuitable for the characterization of inhibitor complexes.
Structure of recombinant Leishmania donovani pteridine reductase reveals a disordered active site.,Barrack KL, Tulloch LB, Burke LA, Fyfe PK, Hunter WN Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jan 1;67(Pt, 1):33-7. Epub 2010 Dec 21. PMID:21206018[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Barrack KL, Tulloch LB, Burke LA, Fyfe PK, Hunter WN. Structure of recombinant Leishmania donovani pteridine reductase reveals a disordered active site. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jan 1;67(Pt, 1):33-7. Epub 2010 Dec 21. PMID:21206018 doi:10.1107/S174430911004724X
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