5mx8
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of H. pylori purine nucleoside phosphorylase from clinical isolate HpPNP-3== | |
| + | <StructureSection load='5mx8' size='340' side='right' caption='[[5mx8]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5mx8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MX8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MX8 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HPA:HYPOXANTHINE'>HPA</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5mx4|5mx4]], [[5mx6|5mx6]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Purine-nucleoside_phosphorylase Purine-nucleoside phosphorylase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5mx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mx8 OCA], [http://pdbe.org/5mx8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mx8 RCSB], [http://www.ebi.ac.uk/pdbsum/5mx8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mx8 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Microaerophilic bacterium Helicobacer pylori is a well known human pathogen involved in the development of many diseases. Due to the evergrowing infection rate and increase of H. pylori antibiotic resistence, it is of utmost importance to find a new way to attack and eradicate H. pylori. The purine metabolism in H. pylori is solely dependant on the salvage pathway and one of the key enzymes in this pathway is purine nucleoside phosphorylase (PNP). In this timely context, we report here the basic biochemical and structural characterization of recombinant PNP from the H. pylori clinical isolate expressed in Escherichia coli. Structure of H. pylori PNP is typical for high molecular mass PNPs. However, its activity towards adenosine is very low, thus resembling more that of low molecular mass PNPs. Understanding the molecular mechanism of this key enzyme may lead to the development of new drug strategies and help in the eradication of H. pylori. | ||
| - | + | Structural characterization of purine nucleoside phosphorylase from human pathogen Helicobacter pylori.,Stefanic Z, Mikleusevic G, Luic M, Bzowska A, Lescic Asler I Int J Biol Macromol. 2017 Mar 20;101:518-526. doi:, 10.1016/j.ijbiomac.2017.03.101. PMID:28336275<ref>PMID:28336275</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5mx8" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Helicobacter pylori]] | ||
| + | [[Category: Purine-nucleoside phosphorylase]] | ||
[[Category: Stefanic, Z]] | [[Category: Stefanic, Z]] | ||
| + | [[Category: Clinical isolate]] | ||
| + | [[Category: Dead-end-complex]] | ||
| + | [[Category: Purine nucleoside phosphorylase]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 13:20, 5 April 2017
Crystal structure of H. pylori purine nucleoside phosphorylase from clinical isolate HpPNP-3
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