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1sq6

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(New page: 200px<br /><applet load="1sq6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sq6, resolution 2.40&Aring;" /> '''Plasmodium falciparu...)
Current revision (08:34, 1 May 2024) (edit) (undo)
 
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[[Image:1sq6.gif|left|200px]]<br /><applet load="1sq6" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1sq6, resolution 2.40&Aring;" />
 
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'''Plasmodium falciparum homolog of Uridine phosphorylase/Purine nucleoside phosphorylase'''<br />
 
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==Overview==
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==Plasmodium falciparum homolog of Uridine phosphorylase/Purine nucleoside phosphorylase==
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Purine metabolism in the parasite Plasmodium has been identified as a, promising target for antimalarial therapies. Purine nucleoside, phosphorylase (PNP) is part of a salvage pathway for the biosynthesis of, purines, which are essential for parasite survival. Two crystal structures, of PNP from Plasmodium falciparum (PfPNP) in two space groups, each with a, single subunit in the asymmetric unit, are described here. One structure, refined to 2.4 A, has an empty nucleoside-binding site and a sulfate ion, bound in the phosphate-binding pocket. The second structure, refined to, 2.0 A, has the substrate inosine bound to the active centre. Structure, comparison reveals alterations in the active site upon ligand binding. The, new structures presented here specifically highlight the likely roles of, Asp206 and two loops flanking the active site: the beta7-alpha6 loop, (residues approximately 161-169) and the beta9-alpha8 loop (residues, approximately 208-223). Comparison with PNP in complex with, transition-state inhibitors suggests that the purine substrate moves, towards the phosphate substrate, rather than vice versa, upon forming the, transition state. The single-substrate-containing PfPNP structures also, appear to be more flexible than PfPNP bound to inhibitors. Together, these, structures serve as a basis for better understanding of ligand binding and, mechanism that can be further exploited to optimize the specificity of, anti-PfPNP drugs.
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<StructureSection load='1sq6' size='340' side='right'caption='[[1sq6]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1sq6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SQ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SQ6 FirstGlance]. <br>
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1SQ6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum_3d7 Plasmodium falciparum 3d7] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Uridine_phosphorylase Uridine phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.3 2.4.2.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SQ6 OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sq6 OCA], [https://pdbe.org/1sq6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sq6 RCSB], [https://www.ebi.ac.uk/pdbsum/1sq6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sq6 ProSAT]</span></td></tr>
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Structures of Plasmodium falciparum purine nucleoside phosphorylase complexed with sulfate and its natural substrate inosine., Schnick C, Robien MA, Brzozowski AM, Dodson EJ, Murshudov GN, Anderson L, Luft JR, Mehlin C, Hol WG, Brannigan JA, Wilkinson AJ, Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1245-54. Epub 2005, Aug 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16131758 16131758]
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</table>
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[[Category: Plasmodium falciparum 3d7]]
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== Function ==
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[[Category: Single protein]]
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[https://www.uniprot.org/uniprot/PNPH_PLAF7 PNPH_PLAF7] As part of the purine salvage pathway, catalyzes 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 (PubMed:18957439, PubMed:14982926, PubMed:16131758, PubMed:19575810, PubMed:24416224, PubMed:29440412). Preferentially acts on inosine and guanosine, and to a lesser extent on 2'-deoxyguanosine and guanosine (PubMed:14982926, PubMed:16131758, PubMed:19575810). Also catalyzes the phosphorylation of S-methyl-5'-thioinosine (MTI) to hypoxanthine; MTI is produced by adenosine deaminase (ADA)-mediated breakdown of S-methyl-5'-thioadenosine (MTA), a major by-product of polyamine biosynthesis (PubMed:18957439, PubMed:14982926, PubMed:24416224). Generates hypoxanthine from both the purine salvage pathway and from polyamine metabolism which is required for nucleic acids synthesis (PubMed:18957439, PubMed:14982926, PubMed:24416224). Has no activity towards adenosine (By similarity).[UniProtKB:Q8T9Z7]<ref>PMID:14982926</ref> <ref>PMID:16131758</ref> <ref>PMID:18957439</ref> <ref>PMID:19575810</ref> <ref>PMID:24416224</ref> <ref>PMID:29440412</ref>
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[[Category: Uridine phosphorylase]]
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== Evolutionary Conservation ==
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[[Category: Hol, W.G.J.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Robien, M.A.]]
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Check<jmol>
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[[Category: SGPP, Structural.Genomics.of.Pathogenic.Protozoa.Consortium.]]
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<jmolCheckbox>
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[[Category: SO4]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sq/1sq6_consurf.spt"</scriptWhenChecked>
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[[Category: alpha+beta]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: protein structure initiative]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: psi]]
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</jmolCheckbox>
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[[Category: sgpp]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1sq6 ConSurf].
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[[Category: structural genomics]]
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<div style="clear:both"></div>
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[[Category: structural genomics of pathogenic protozoa consortium]]
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== References ==
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<references/>
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:59:22 2007''
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Plasmodium falciparum 3D7]]
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[[Category: Hol WGJ]]
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[[Category: Robien MA]]

Current revision

Plasmodium falciparum homolog of Uridine phosphorylase/Purine nucleoside phosphorylase

PDB ID 1sq6

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