4zo3: Difference between revisions
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The | ==AidC, a Dizinc Quorum-Quenching Lactonase, in complex with a product N-hexnoyl-L-homoserine== | ||
<StructureSection load='4zo3' size='340' side='right'caption='[[4zo3]], [[Resolution|resolution]] 1.67Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4zo3]] 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=4ZO3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZO3 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]] 1.67Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C6L:N-HEXANOYL-L-HOMOSERINE'>C6L</scene>, <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=4zo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zo3 OCA], [https://pdbe.org/4zo3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zo3 RCSB], [https://www.ebi.ac.uk/pdbsum/4zo3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zo3 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. >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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 4zo3" style="background-color:#fffaf0;"></div> | ||
[[Category: Hoang | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Chryseobacterium sp. StRB126]] | ||
[[Category: | [[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]] | |||
Latest revision as of 11:21, 27 September 2023
AidC, a Dizinc Quorum-Quenching Lactonase, in complex with a product N-hexnoyl-L-homoserineAidC, a Dizinc Quorum-Quenching Lactonase, in complex with a product N-hexnoyl-L-homoserine
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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