5oe0: Difference between revisions

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 ==CRYSTAL STRUCTURE OF THE BETA-LACTAMASE OXA-181==
-<StructureSection load='5oe0' size='340' side='right' caption='[[5oe0]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
+<StructureSection load='5oe0' size='340' side='right'caption='[[5oe0]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5oe0]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OE0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OE0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5oe0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OE0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OE0 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.0500083&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </span></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=5oe0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oe0 OCA], [https://pdbe.org/5oe0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oe0 RCSB], [https://www.ebi.ac.uk/pdbsum/5oe0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oe0 ProSAT]</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=5oe0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oe0 OCA], [http://pdbe.org/5oe0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oe0 RCSB], [http://www.ebi.ac.uk/pdbsum/5oe0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oe0 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/G5CKK8_KLEPN G5CKK8_KLEPN]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The first crystal structures of the class D beta-lactamases OXA-181 and OXA-245 were determined to 2.05 and 2.20 A resolution, respectively; in addition, the structure of a new crystal form of OXA-163 was resolved to 2.07 A resolution. All of these enzymes are OXA-48-like and have been isolated from different clinical Klebsiella pneumoniae strains and also from other human pathogens such as Pseudomonas aeruginosa and Escherichia coli. Here, enzyme kinetics and thermostability studies are presented, and the new crystal structures are used to explain the observed variations. OXA-245 had the highest melting point (Tm = 55.8 degrees C), as determined by differential scanning calorimetry, compared with OXA-163 (Tm = 49.4 degrees C) and OXA-181 (Tm = 52.6 degrees C). The differences could be explained by the loss of two salt bridges in OXA-163, and an overall decrease in the polarity of the surface of OXA-181 compared with OXA-245.
+Structure, activity and thermostability investigations of OXA-163, OXA-181 and OXA-245 using biochemical analysis, crystal structures and differential scanning calorimetry analysis.,Lund BA, Thomassen AM, Carlsen TJO, Leiros HKS Acta Crystallogr F Struct Biol Commun. 2017 Oct 1;73(Pt 10):579-587. doi:, 10.1107/S2053230X17013838. Epub 2017 Oct 2. PMID:28994407<ref>PMID:28994407</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5oe0" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>
-[[Category: Beta-lactamase]]
+[[Category: Klebsiella pneumoniae]]
-[[Category: Carlsen, T J.O]]
+[[Category: Large Structures]]
-[[Category: Leiros, H K.S]]
+[[Category: Carlsen TJO]]
-[[Category: Lund, B A]]
+[[Category: Leiros HKS]]
-[[Category: Thomassen, A M]]
+[[Category: Lund BA]]
-[[Category: Antibiotic]]
+[[Category: Thomassen AM]]
-[[Category: Antibiotic resistance]]
-[[Category: Carbapenemase]]
-[[Category: Oxa-48-like]]
-[[Category: Oxacillinase]]