7op9: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 7op9 is ON HOLD
+==Purine nucleoside phosphorylase(DeoD-type) from H. pylori with 2,6-dichloropurine==
+<StructureSection load='7op9' size='340' side='right'caption='[[7op9]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7op9]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OP9 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]] 1.5&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=06K:2,6-bis(chloranyl)-7H-purine'>06K</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</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=7op9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7op9 OCA], [https://pdbe.org/7op9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7op9 RCSB], [https://www.ebi.ac.uk/pdbsum/7op9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7op9 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/DEOD_HELPY DEOD_HELPY]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Helicobacter pylori represents a global health threat with around 50% of the world population infected. Due to the increasing number of antibiotic-resistant strains, new strategies for eradication of H. pylori are needed. In this study, we suggest purine nucleoside phosphorylase (PNP) as a possible new drug target, by characterising its interactions with 2- and/or 6-substituted purines as well as the effect of these compounds on bacterial growth. Inhibition constants are in the micromolar range, the lowest being that of 6-benzylthio-2-chloropurine. This compound also inhibits H. pylori 26695 growth at the lowest concentration. X-ray structures of the complexes of PNP with the investigated compounds allowed the identification of interactions of inhibitors in the enzyme's base-binding site and the suggestion of structures that could bind to the enzyme more tightly. Our findings prove the potential of PNP inhibitors in the design of drugs against H. pylori.
-Authors:
+Interactions of 2,6-substituted purines with purine nucleoside phosphorylase from Helicobacter pylori in solution and in the crystal, and the effects of these compounds on cell cultures of this bacterium.,Narczyk M, Wojtys MI, Lescic Asler I, Zinic B, Luic M, Jagusztyn-Krynicka EK, Stefanic Z, Bzowska A J Enzyme Inhib Med Chem. 2022 Dec;37(1):1083-1097. doi:, 10.1080/14756366.2022.2061965. PMID:35437103<ref>PMID:35437103</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 7op9" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Purine nucleoside phosphorylase 3D structures|Purine nucleoside phosphorylase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Helicobacter pylori 26695]]
+[[Category: Large Structures]]
+[[Category: Narczyk M]]
+[[Category: Stefanic Z]]