4bd0: Difference between revisions
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==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]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli BL21]] | |||
[[Category: Large Structures]] | |||
[[Category: Coates L]] | |||
[[Category: Ng JD]] | |||
[[Category: Ostermann A]] | |||
[[Category: Schrader TE]] | |||
[[Category: Standaert RF]] | |||
[[Category: Tomanicek SJ]] | |||
[[Category: Weiss KL]] | |||
Latest revision as of 14:48, 20 December 2023
X-ray structure of a perdeuterated Toho-1 R274N R276N double mutant Beta-lactamase in complex with a fully deuterated boronic acid (BZB)X-ray structure of a perdeuterated Toho-1 R274N R276N double mutant Beta-lactamase in complex with a fully deuterated boronic acid (BZB)
Structural highlights
FunctionBLT1_ECOLX Has strong cefotaxime-hydrolyzing activity. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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