7oda: Difference between revisions
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<StructureSection load='7oda' size='340' side='right'caption='[[7oda]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='7oda' size='340' side='right'caption='[[7oda]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7oda]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.796Å</td></tr> | ||
<tr id=' | <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> | <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> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0S2C593_ENTAS A0A0S2C593_ENTAS] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 7oda" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 7oda" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Enterobacter asburiae]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Carlsen | [[Category: Carlsen TJW]] | ||
[[Category: Leiros | [[Category: Leiros HKS]] | ||
[[Category: Lund | [[Category: Lund BA]] | ||
[[Category: Thomassen | [[Category: Thomassen AM]] | ||
Latest revision as of 15:49, 1 February 2024
OXA-48-like Beta-lactamase OXA-436OXA-48-like Beta-lactamase OXA-436
Structural highlights
FunctionPublication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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