View source for 4g8d


==Crystal structures of N-acyl homoserine lactonase AidH S102G mutant==
<StructureSection load='4g8d' size='340' side='right'caption='[[4g8d]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4g8d]] 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=4G8D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G8D 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]] 1.35&#8491;</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=4g8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g8d OCA], [https://pdbe.org/4g8d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g8d RCSB], [https://www.ebi.ac.uk/pdbsum/4g8d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g8d ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D2J2T6_9HYPH D2J2T6_9HYPH] 
<div style="background-color:#fffaf0;">
== 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>
</div>
<div class="pdbe-citations 4g8d" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Ochrobactrum sp. T63]]
[[Category: Gao A]]
[[Category: Liang DC]]
[[Category: Yan XX]]