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==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]] 2.00Å' 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®/PubMed®, 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: Beta-lactamase]] | ||
[[Category: | [[Category: Ecobb]] | ||
[[Category: Coates, L | [[Category: Large Structures]] | ||
[[Category: Ng, J D | [[Category: Coates, L]] | ||
[[Category: Ostermann, A | [[Category: Ng, J D]] | ||
[[Category: Schrader, T E | [[Category: Ostermann, A]] | ||
[[Category: Standaert, R F | [[Category: Schrader, T E]] | ||
[[Category: Tomanicek, S J | [[Category: Standaert, R F]] | ||
[[Category: Weiss, K L | [[Category: Tomanicek, S J]] | ||
[[Category: Weiss, K L]] | |||
[[Category: Ctx- m-type esbl]] | [[Category: Ctx- m-type esbl]] | ||
[[Category: Extended-spectrum beta lactamase]] | [[Category: Extended-spectrum beta lactamase]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Perdeuterated neutron structure]] | [[Category: Perdeuterated neutron structure]] | ||
Latest revision as of 10:08, 31 August 2022
Neutron structure of a perdeuterated Toho-1 R274N R276N double mutant Beta-lactamase in complex with a fully deuterated boronic acid (BZB)Neutron structure of a perdeuterated Toho-1 R274N R276N double mutant Beta-lactamase in complex with a fully deuterated boronic acid (BZB)
Structural highlights
Function[BLT1_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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