8swp
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of K. lactis PNP bound to hypoxanthine== | |
| + | <StructureSection load='8swp' size='340' side='right'caption='[[8swp]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8swp]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Kluyveromyces_lactis_NRRL_Y-1140 Kluyveromyces lactis NRRL Y-1140]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8SWP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SWP 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]] 2.1Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=HPA:HYPOXANTHINE'>HPA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=8swp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8swp OCA], [https://pdbe.org/8swp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8swp RCSB], [https://www.ebi.ac.uk/pdbsum/8swp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8swp ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q6CSZ6_KLULA Q6CSZ6_KLULA] 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.[PIRNR:PIRNR000477] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Purine nucleoside phosphorylases (PNPs) catalyze the phosphorolysis of 6-oxypurine nucleosides with an HPO(4)(2-) dianion nucleophile. Nucleosides and phosphate occupy distinct pockets in the PNP active site. Evaluation of the HPO(4)(2-) site by mutagenesis, cooperative binding studies, and thermodynamic and structural analysis demonstrate that alterations in the HPO(4)(2-) binding site can render PNP inactive and significantly impact subunit cooperativity and binding to transition-state analogue inhibitors. Cooperative interactions between the cationic transition-state analogue and the anionic HPO(4)(2-) nucleophile demonstrate the importance of reforming the transition-state ensemble for optimal inhibition with transition-state analogues. Altered phosphate binding in the catalytic site mutants helps to explain one of the known lethal PNP deficiency syndromes in humans. | ||
| - | + | Phosphate Binding in PNP Alters Transition-State Analogue Affinity and Subunit Cooperativity.,Minnow YVT, Schramm VL, Almo SC, Ghosh A Biochemistry. 2023 Nov 7;62(21):3116-3125. doi: 10.1021/acs.biochem.3c00264. Epub , 2023 Oct 9. PMID:37812583<ref>PMID:37812583</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Fedorov | + | <div class="pdbe-citations 8swp" style="background-color:#fffaf0;"></div> |
| - | [[Category: Ghosh | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Kluyveromyces lactis NRRL Y-1140]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Fedorov E]] | ||
| + | [[Category: Ghosh A]] | ||
Current revision
Structure of K. lactis PNP bound to hypoxanthine
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