View source for 4zo2


==AidC, a Dizinc Quorum-Quenching Lactonase==
<StructureSection load='4zo2' size='340' side='right'caption='[[4zo2]], [[Resolution|resolution]] 1.09&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4zo2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chryseobacterium_sp._StRB126 Chryseobacterium sp. StRB126]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZO2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZO2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4zo2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zo2 OCA], [https://pdbe.org/4zo2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zo2 RCSB], [https://www.ebi.ac.uk/pdbsum/4zo2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zo2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/I7HB71_9FLAO I7HB71_9FLAO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Quorum-quenching catalysts are of interest for potential application as biochemical tools for interrogating interbacterial communication pathways, as antibiofouling agents, and as anti-infective agents in plants and animals. Herein, the structure and function of AidC, an N-acyl-l-homoserine lactone (AHL) lactonase from Chryseobacterium, is characterized. Steady-state kinetics show that zinc-supplemented AidC is the most efficient wild-type quorum-quenching enzymes characterized to date, with a kcat/KM value of approximately 2 x 106 M-1 s-1 for N-heptanoyl-l-homoserine lactone. The enzyme has stricter substrate selectivity and significantly lower KM values (ca. 50 muM for preferred substrates) compared to those of typical AHL lactonases (ca. &gt;1 mM). X-ray crystal structures of AidC alone and with the product N-hexanoyl-l-homoserine were determined at resolutions of 1.09 and 1.67 A, respectively. Each structure displays as a dimer, and dimeric oligiomerization was also observed in solution by size-exclusion chromatography coupled with multiangle light scattering. The structures reveal two atypical features as compared to previously characterized AHL lactonases: a "kinked" alpha-helix that forms part of a closed binding pocket that provides affinity and enforces selectivity for AHL substrates and an active-site His substitution that is usually found in a homologous family of phosphodiesterases. Implications for the catalytic mechanism of AHL lactonases are discussed.

Structural and Biochemical Characterization of AidC, a Quorum-Quenching Lactonase with Atypical Selectivity.,Mascarenhas R, Thomas PW, Wu CX, Nocek BP, Hoang QQ, Liu D, Fast W Biochemistry. 2015 Jul 8. PMID:26115006<ref>PMID:26115006</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4zo2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chryseobacterium sp. StRB126]]
[[Category: Large Structures]]
[[Category: Fast W]]
[[Category: Hoang Q]]
[[Category: Liu D]]
[[Category: Mascarenhas R]]
[[Category: Nocek BP]]
[[Category: Thomas PW]]
[[Category: Wu C-X]]