4g5x

</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>

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== Publication Abstract from PubMed ==

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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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