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| | ==Crystal structures of N-acyl homoserine lactonase AidH== | | ==Crystal structures of N-acyl homoserine lactonase AidH== |
| - | <StructureSection load='4g5x' size='340' side='right' caption='[[4g5x]], [[Resolution|resolution]] 1.29Å' scene=''> | + | <StructureSection load='4g5x' size='340' side='right'caption='[[4g5x]], [[Resolution|resolution]] 1.29Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4g5x]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ochrobactrum_sp._t63 Ochrobactrum sp. t63]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G5X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G5X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4g5x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ochrobactrum_sp._T63 Ochrobactrum sp. T63]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G5X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G5X FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4g8b|4g8b]], [[4g8c|4g8c]], [[4g8d|4g8d]], [[4g9e|4g9e]], [[4g9g|4g9g]]</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]] 1.29Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aidH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=680275 Ochrobactrum sp. T63])</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=4g5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g5x OCA], [https://pdbe.org/4g5x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g5x RCSB], [https://www.ebi.ac.uk/pdbsum/4g5x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g5x 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=4g5x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g5x OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g5x RCSB], [http://www.ebi.ac.uk/pdbsum/4g5x PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/D2J2T6_9HYPH D2J2T6_9HYPH] |
| - | Many pathogenic bacteria that infect humans, animals and plants rely on a quorum-sensing (QS) system to produce virulence factors. N-Acyl homoserine lactones (AHLs) are the best-characterized cell-cell communication signals in QS. The concentration of AHL plays a key role in regulating the virulence-gene expression and essential biological functions of pathogenic bacteria. N-Acyl homoserine lactonases (AHL-lactonases) have important functions in decreasing pathogenicity by degrading AHLs. Here, structures of the AHL-lactonase from Ochrobactrum sp. (AidH) in complex with N-hexanoyl homoserine lactone, N-hexanoyl homoserine and N-butanoyl homoserine are reported. The high-resolution structures together with biochemical analyses reveal convincing details of AHL degradation. No metal ion is bound in the active site, which is different from other AHL-lactonases, which have a dual Lewis acid catalysis mechanism. AidH contains a substrate-binding tunnel between the core domain and the cap domain. The conformation of the tunnel entrance varies with the AHL acyl-chain length, which contributes to the binding promiscuity of AHL molecules in the active site. It also supports the biochemical result that AidH is a broad catalytic spectrum AHL-lactonase. Taken together, the present results reveal the catalytic mechanism of the metal-independent AHL-lactonase, which is a typical acid-base covalent catalysis.
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| - | High-resolution structures of AidH complexes provide insights into a novel catalytic mechanism for N-acyl homoserine lactonase.,Gao A, Mei GY, Liu S, Wang P, Tang Q, Liu YP, Wen H, An XM, Zhang LQ, Yan XX, Liang DC Acta Crystallogr D Biol Crystallogr. 2013 Jan;69(Pt 1):82-91. doi:, 10.1107/S0907444912042369. Epub 2012 Dec 20. PMID:23275166<ref>PMID:23275166</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | == References ==
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| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ochrobactrum sp. t63]] | + | [[Category: Large Structures]] |
| - | [[Category: Gao, A]] | + | [[Category: Ochrobactrum sp. T63]] |
| - | [[Category: Liang, D C]] | + | [[Category: Gao A]] |
| - | [[Category: Yan, X X]] | + | [[Category: Liang DC]] |
| - | [[Category: Alpha/beta-hydrolase fold]]
| + | [[Category: Yan XX]] |
| - | [[Category: Core domain]]
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| - | [[Category: Eight-stranded sheet]]
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| - | [[Category: Hydrolase]]
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| - | [[Category: Lactonase]]
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