4zo3: Difference between revisions
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==AidC, a Dizinc Quorum-Quenching Lactonase, in complex with a product N-hexnoyl-L-homoserine== | ==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=''> | <StructureSection load='4zo3' size='340' side='right'caption='[[4zo3]], [[Resolution|resolution]] 1.67Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4zo3]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZO3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4zo3]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZO3 FirstGlance]. <br> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Chryseobacterium sp. strb126]] | [[Category: Chryseobacterium sp. strb126]] | ||
[[Category: Large Structures]] | |||
[[Category: Fast, W]] | [[Category: Fast, W]] | ||
[[Category: Hoang, Q]] | [[Category: Hoang, Q]] | ||
Revision as of 10:25, 27 November 2019
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
Publication 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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