5mx4: Difference between revisions
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<StructureSection load='5mx4' size='340' side='right'caption='[[5mx4]], [[Resolution|resolution]] 2.31Å' scene=''> | <StructureSection load='5mx4' size='340' side='right'caption='[[5mx4]], [[Resolution|resolution]] 2.31Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5mx4]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5mx4]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_R018c Helicobacter pylori R018c]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MX4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MX4 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.31Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HPA:HYPOXANTHINE'>HPA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5mx4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mx4 OCA], [https://pdbe.org/5mx4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mx4 RCSB], [https://www.ebi.ac.uk/pdbsum/5mx4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mx4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/K2JXG0_HELPX K2JXG0_HELPX] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Helicobacter pylori | [[Category: Helicobacter pylori R018c]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Stefanic Z]] | |||
[[Category: Stefanic | |||
Latest revision as of 20:52, 8 November 2023
Crystal structure of H. pylori purine nucleoside phosphorylase from clinical isolate HpPNP-1Crystal structure of H. pylori purine nucleoside phosphorylase from clinical isolate HpPNP-1
Structural highlights
FunctionPublication Abstract from PubMedMicroaerophilic 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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