5mx4: 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 5mx4 is ON HOLD
+==Crystal structure of H. pylori purine nucleoside phosphorylase from clinical isolate HpPNP-1==
+<StructureSection load='5mx4' size='340' side='right'caption='[[5mx4]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
+== Structural highlights ==
+<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.31&#8491;</td></tr>
+<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'>[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>
+== Function ==
+[https://www.uniprot.org/uniprot/K2JXG0_HELPX K2JXG0_HELPX]
+<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.
-Authors: Stefanic, Z.
+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>
-Description: Crystal structure of H. pylori purine nucleoside phosphorylase from clinical isolate HpPNP-1
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Stefanic, Z]]
+<div class="pdbe-citations 5mx4" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Purine nucleoside phosphorylase 3D structures|Purine nucleoside phosphorylase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Helicobacter pylori R018c]]
+[[Category: Large Structures]]
+[[Category: Stefanic Z]]