7oda: Difference between revisions

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OCA

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-'''Unreleased structure'''
-The entry 7oda is ON HOLD
+==OXA-48-like Beta-lactamase OXA-436==
+<StructureSection load='7oda' size='340' side='right'caption='[[7oda]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7oda]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacter_asburiae Enterobacter asburiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ODA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ODA 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]] 1.796&#8491;</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</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=7oda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oda OCA], [https://pdbe.org/7oda PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oda RCSB], [https://www.ebi.ac.uk/pdbsum/7oda PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oda ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/A0A0S2C593_ENTAS A0A0S2C593_ENTAS]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The crystal structure of the class D beta-lactamase OXA-436 was solved to a resolution of 1.80 A. Higher catalytic rates were found at higher temperatures for the clinically important antibiotic imipenem, indicating better adaptation of OXA-436 to its mesophilic host than OXA-48, which is believed to originate from an environmental source. Furthermore, based on the most populated conformations during 100 ns molecular-dynamics simulations, it is postulated that the modulation of activity involves conformational shifts of the alpha3-alpha4 and beta5-beta6 loops. While these changes overall do not cause clinically significant shifts in the resistance profile, they show that antibiotic-resistance enzymes exist in a continuum. It is believed that these seemingly neutral differences in the sequence exist on a path leading to significant changes in substrate selectivity.
-Authors: Lund, B.A., Thomassen, A.M., Carlsen, T.J.W., Leiros, H.K.S.
+Biochemical and biophysical characterization of the OXA-48-like carbapenemase OXA-436.,Lund BA, Thomassen AM, Carlsen TJW, Leiros HKS Acta Crystallogr F Struct Biol Commun. 2021 Sep 1;77(Pt 9):312-318. doi:, 10.1107/S2053230X21008645. Epub 2021 Aug 31. PMID:34473108<ref>PMID:34473108</ref>
-Description: OXA-48-like Beta-lactamase OXA-436
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Leiros, H.K.S]]
+<div class="pdbe-citations 7oda" style="background-color:#fffaf0;"></div>
-[[Category: Carlsen, T.J.W]]
-[[Category: Lund, B.A]]
+==See Also==
-[[Category: Thomassen, A.M]]
+*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Enterobacter asburiae]]
+[[Category: Large Structures]]
+[[Category: Carlsen TJW]]
+[[Category: Leiros HKS]]
+[[Category: Lund BA]]
+[[Category: Thomassen AM]]