This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
7oda
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==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
| |||||||||||
