7oda
From Proteopedia
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==OXA-48-like Beta-lactamase OXA-436== | ==OXA-48-like Beta-lactamase OXA-436== | ||
| - | <StructureSection load='7oda' size='340' side='right'caption='[[7oda]]' scene=''> | + | <StructureSection load='7oda' size='340' side='right'caption='[[7oda]], [[Resolution|resolution]] 1.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>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> | + | <table><tr><td colspan='2'>[[7oda]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35953 Atcc 35953]. 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='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> | + | </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></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">blaOXA-436 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=61645 ATCC 35953])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [https://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=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> | </table> | ||
| + | <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. | ||
| + | |||
| + | 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> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7oda" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Atcc 35953]] | ||
| + | [[Category: Beta-lactamase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Carlsen | + | [[Category: Carlsen, T J.W]] |
| - | [[Category: Leiros | + | [[Category: Leiros, H K.S]] |
| - | [[Category: Lund | + | [[Category: Lund, B A]] |
| - | [[Category: Thomassen | + | [[Category: Thomassen, A M]] |
| + | [[Category: Antibiotic resistance]] | ||
| + | [[Category: Hydrolase]] | ||
Revision as of 12:56, 13 October 2021
OXA-48-like Beta-lactamase OXA-436
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