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2xqz
From Proteopedia
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| - | [[Image:2xqz.png|left|200px]] | ||
| - | + | ==Neutron structure of the perdeuterated Toho-1 R274N R276N double mutant beta-lactamase== | |
| + | <StructureSection load='2xqz' size='340' side='right'caption='[[2xqz]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2xqz]] 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=2XQZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XQZ FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Neutron Diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</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=2xqz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xqz OCA], [https://pdbe.org/2xqz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xqz RCSB], [https://www.ebi.ac.uk/pdbsum/2xqz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xqz ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/BLT1_ECOLX BLT1_ECOLX] Has strong cefotaxime-hydrolyzing activity. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Room 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<ref>PMID:21168411</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2xqz" style="background-color:#fffaf0;"></div> | |
| - | + | ||
==See Also== | ==See Also== | ||
| - | *[[Beta-lactamase|Beta-lactamase]] | + | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: Blakeley | + | [[Category: Large Structures]] |
| - | [[Category: Chen | + | [[Category: Blakeley MP]] |
| - | [[Category: Coates | + | [[Category: Chen Y]] |
| - | [[Category: Cooper | + | [[Category: Coates L]] |
| - | [[Category: Tomanicek | + | [[Category: Cooper J]] |
| - | [[Category: Wang | + | [[Category: Tomanicek SJ]] |
| - | [[Category: Weiss | + | [[Category: Wang KK]] |
| - | + | [[Category: Weiss KL]] | |
| - | + | ||
Current revision
Neutron structure of the perdeuterated Toho-1 R274N R276N double mutant beta-lactamase
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Categories: Escherichia coli | Large Structures | Blakeley MP | Chen Y | Coates L | Cooper J | Tomanicek SJ | Wang KK | Weiss KL
