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| | <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 [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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C6L:N-HEXANOYL-L-HOMOSERINE'>C6L</scene>, <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]] 1.67Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4zo2|4zo2]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aidC, CHSO_3121 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=878220 Chryseobacterium sp. StRB126])</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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4zo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zo3 OCA], [http://pdbe.org/4zo3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zo3 RCSB], [http://www.ebi.ac.uk/pdbsum/4zo3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zo3 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/I7HB71_9FLAO I7HB71_9FLAO] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chryseobacterium sp. strb126]] | + | [[Category: Chryseobacterium sp. StRB126]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fast, W]] | + | [[Category: Fast W]] |
| - | [[Category: Hoang, Q]] | + | [[Category: Hoang Q]] |
| - | [[Category: Liu, D]] | + | [[Category: Liu D]] |
| - | [[Category: Mascarenhas, R]] | + | [[Category: Mascarenhas R]] |
| - | [[Category: Nocek, B P]] | + | [[Category: Nocek BP]] |
| - | [[Category: Thomas, P W]] | + | [[Category: Thomas PW]] |
| - | [[Category: Wu, C X]] | + | [[Category: Wu C-X]] |
| - | [[Category: Aidc]]
| + | |
| - | [[Category: Dizinc]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Lactonase]]
| + | |
| - | [[Category: N-acyl-l-homoserine]]
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| - | [[Category: Quorum-quenching]]
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| Structural highlights
Function
I7HB71_9FLAO
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mascarenhas R, Thomas PW, Wu CX, Nocek BP, Hoang QQ, Liu D, Fast W. Structural and Biochemical Characterization of AidC, a Quorum-Quenching Lactonase with Atypical Selectivity. Biochemistry. 2015 Jul 8. PMID:26115006 doi:http://dx.doi.org/10.1021/acs.biochem.5b00499
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