4bd0
From Proteopedia
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| - | [[Image:4bd0.png|left|200px]] | ||
| - | + | ==X-ray structure of a perdeuterated Toho-1 R274N R276N double mutant Beta-lactamase in complex with a fully deuterated boronic acid (BZB)== | |
| + | <StructureSection load='4bd0' size='340' side='right'caption='[[4bd0]], [[Resolution|resolution]] 1.21Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4bd0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21 Escherichia coli BL21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BD0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BD0 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.207Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BZB:BENZO[B]THIOPHENE-2-BORONIC+ACID'>BZB</scene>, <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=4bd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bd0 OCA], [https://pdbe.org/4bd0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bd0 RCSB], [https://www.ebi.ac.uk/pdbsum/4bd0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bd0 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 == | ||
| + | The mechanism by which class A beta-lactamase enzymes form an acyl-enzyme intermediate has been the emphasis of several studies. Here, we report on the use of neutron and high resolution X-ray diffraction to help elucidate the identity of the catalytic base in the acylation part of the mechanism. | ||
| - | + | Neutron and X-ray crystal structures of a perdeuterated enzyme inhibitor complex reveal the catalytic proton network of the Toho-1 beta-lactamase for the acylation reaction.,Tomanicek SJ, Standaert RF, Weiss KL, Ostermann A, Schrader TE, Ng JD, Coates L J Biol Chem. 2012 Dec 18. PMID:23255594<ref>PMID:23255594</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4bd0" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | [[ | + | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: Coates | + | __TOC__ |
| - | [[Category: Ng | + | </StructureSection> |
| - | [[Category: Ostermann | + | [[Category: Escherichia coli BL21]] |
| - | [[Category: Schrader | + | [[Category: Large Structures]] |
| - | [[Category: Standaert | + | [[Category: Coates L]] |
| - | [[Category: Tomanicek | + | [[Category: Ng JD]] |
| - | [[Category: Weiss | + | [[Category: Ostermann A]] |
| - | + | [[Category: Schrader TE]] | |
| - | + | [[Category: Standaert RF]] | |
| - | + | [[Category: Tomanicek SJ]] | |
| - | + | [[Category: Weiss KL]] | |
Current revision
X-ray structure of a perdeuterated Toho-1 R274N R276N double mutant Beta-lactamase in complex with a fully deuterated boronic acid (BZB)
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