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== | ==Room temperature X-ray structure of the perdeuterated Toho-1 R274N R276N double mutant beta-lactamase== | ||
<StructureSection load='2xr0' size='340' side='right' caption='[[2xr0]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='2xr0' size='340' side='right'caption='[[2xr0]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2xr0]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2xr0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XR0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XR0 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]] 2.2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2xr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xr0 OCA], [https://pdbe.org/2xr0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xr0 RCSB], [https://www.ebi.ac.uk/pdbsum/2xr0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xr0 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/BLT1_ECOLX BLT1_ECOLX] Has strong cefotaxime-hydrolyzing activity. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 22: | Line 21: | ||
==See Also== | ==See Also== | ||
*[[Beta-lactamase|Beta-lactamase]] | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Blakeley | [[Category: Blakeley MP]] | ||
[[Category: Chen | [[Category: Chen Y]] | ||
[[Category: Coates | [[Category: Coates L]] | ||
[[Category: Cooper | [[Category: Cooper J]] | ||
[[Category: Tomanicek | [[Category: Tomanicek SJ]] | ||
[[Category: Wang | [[Category: Wang KK]] | ||
[[Category: Weiss | [[Category: Weiss KL]] | ||
Latest revision as of 13:37, 20 December 2023
Room temperature X-ray structure of the perdeuterated Toho-1 R274N R276N double mutant beta-lactamaseRoom temperature X-ray structure of the perdeuterated Toho-1 R274N R276N double mutant beta-lactamase
Structural highlights
FunctionBLT1_ECOLX Has strong cefotaxime-hydrolyzing activity. Publication Abstract from PubMedRoom temperature neutron diffraction data of the fully perdeuterated Toho-1 R274N/R276N double mutant beta-lactamase in the apo form were used to visualize deuterium atoms within the active site of the enzyme. This perdeuterated neutron structure of the Toho-1 R274N/R276N reveals the clearest picture yet of the ground-state active site protonation states and the complete hydrogen-bonding network in a beta-lactamase enzyme. The ground-state active site protonation states detailed in this neutron diffraction study are consistent with previous high-resolution X-ray studies that support the role of Glu166 as the general base during the acylation reaction in the class A beta-lactamase reaction pathway. The active site protonation states of perdeuterated Toho-1 beta-lactamase determined by neutron diffraction support a role for Glu166 as the general base in acylation.,Tomanicek SJ, Wang KK, Weiss KL, Blakeley MP, Cooper J, Chen Y, Coates L FEBS Lett. 2010 Dec 17. PMID:21168411[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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