6cgy: Difference between revisions

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<StructureSection load='6cgy' size='340' side='right'caption='[[6cgy]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
<StructureSection load='6cgy' size='340' side='right'caption='[[6cgy]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6cgy]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CGY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6CGY FirstGlance]. <br>
<table><tr><td colspan='2'>[[6cgy]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Alicyclobacillus_acidoterrestris_ATCC_49025 Alicyclobacillus acidoterrestris ATCC 49025]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CGY FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6cgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cgy OCA], [http://pdbe.org/6cgy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cgy RCSB], [http://www.ebi.ac.uk/pdbsum/6cgy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cgy ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=6cgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cgy OCA], [https://pdbe.org/6cgy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cgy RCSB], [https://www.ebi.ac.uk/pdbsum/6cgy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cgy ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/T0BMH6_ALIAG T0BMH6_ALIAG]
Quorum quenching lactonases are enzymes that are capable of disrupting bacterial signaling based on acyl homoserine lactones (AHL) via their enzymatic degradation. In particular, lactonases have therefore been demonstrated to inhibit bacterial behaviors that depend on these chemicals, such as the formation of biofilms or the expression of virulence factors. Here we characterized biochemically and structurally a novel representative from the metallo-beta-lactamase superfamily, named AaL that was isolated from the thermoacidophilic bacterium Alicyclobacillus acidoterrestris. AaL is a potent quorum quenching enzyme as demonstrated by its ability to inhibit the biofilm formation of Acinetobacter baumannii. Kinetic studies demonstrate that AaL is both a proficient and a broad spectrum enzyme, being capable of hydrolyzing a wide range of lactones with high rates (kcat/KM &gt; 10(5) M(-1).s(-1)). Additionally, AaL exhibits unusually low KM values, ranging from 10 to 80 microM. Analysis of AaL structures bound to phosphate, glycerol, and C6-AHL reveals a unique hydrophobic patch (W26, F87 and I237), involved in substrate binding, possibly accounting for the enzyme's high specificity. Identifying the specificity determinants will aid the development of highly specific quorum quenching enzymes as potential therapeutics.
 
Structural and Biochemical Characterization of AaL, a Quorum Quenching Lactonase with Unusual Kinetic Properties.,Bergonzi C, Schwab M, Naik T, Daude D, Chabriere E, Elias M Sci Rep. 2018 Jul 26;8(1):11262. doi: 10.1038/s41598-018-28988-5. PMID:30050039<ref>PMID:30050039</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6cgy" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Alicyclobacillus acidoterrestris ATCC 49025]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bergonzi, C]]
[[Category: Bergonzi C]]
[[Category: Chabriere, E]]
[[Category: Chabriere E]]
[[Category: Daude, D]]
[[Category: Daude D]]
[[Category: Elias, M]]
[[Category: Elias M]]
[[Category: Naik, T]]
[[Category: Naik T]]
[[Category: Schwab, M]]
[[Category: Schwab M]]
[[Category: Acyl homoserine lactone hydrolase]]
[[Category: Hydrolase]]
[[Category: Lactonase]]

Latest revision as of 14:28, 13 March 2024

Structure of the Quorum Quenching lactonase from Alicyclobacillus acidoterrestris bound to a phosphate anion

6cgy, resolution 1.65Å

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