View source for 4bd1


==Neutron structure of a perdeuterated Toho-1 R274N R276N double mutant Beta-lactamase in complex with a fully deuterated boronic acid (BZB)==
<StructureSection load='4bd1' size='340' side='right'caption='[[4bd1]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4bd1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecobb Ecobb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BD1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BD1 FirstGlance]. <br>
</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=DOD:DEUTERATED+WATER'>DOD</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bza|1bza]], [[1iyo|1iyo]], [[1iyp|1iyp]], [[1iyq|1iyq]], [[1iys|1iys]], [[1we4|1we4]], [[2wyx|2wyx]], [[2xqz|2xqz]], [[2xr0|2xr0]], [[4bd0|4bd0]]</div></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=4bd1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bd1 OCA], [https://pdbe.org/4bd1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bd1 RCSB], [https://www.ebi.ac.uk/pdbsum/4bd1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bd1 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4bd1" style="background-color:#fffaf0;"></div>

==See Also==
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Beta-lactamase]]
[[Category: Ecobb]]
[[Category: Large Structures]]
[[Category: Coates, L]]
[[Category: Ng, J D]]
[[Category: Ostermann, A]]
[[Category: Schrader, T E]]
[[Category: Standaert, R F]]
[[Category: Tomanicek, S J]]
[[Category: Weiss, K L]]
[[Category: Ctx- m-type esbl]]
[[Category: Extended-spectrum beta lactamase]]
[[Category: Hydrolase]]
[[Category: Perdeuterated neutron structure]]