4zo2: Difference between revisions
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== Structural highlights == | == 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> | <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> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.09Å</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> | <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> | </table> | ||
Latest revision as of 11:21, 27 September 2023
AidC, a Dizinc Quorum-Quenching LactonaseAidC, a Dizinc Quorum-Quenching Lactonase
Structural highlights
FunctionPublication Abstract from PubMedQuorum-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. >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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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