4g9e: Difference between revisions
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The | ==Crystal structures of N-acyl homoserine lactonase AidH complexed with N-butanoyl homoserine== | ||
<StructureSection load='4g9e' size='340' side='right'caption='[[4g9e]], [[Resolution|resolution]] 1.09Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4g9e]] 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=4G9E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G9E 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]] 1.088Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C4L:N-BUTANOYL-L-HOMOSERINE'>C4L</scene></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=4g9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g9e OCA], [https://pdbe.org/4g9e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g9e RCSB], [https://www.ebi.ac.uk/pdbsum/4g9e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g9e 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4g9e" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Ochrobactrum sp. T63]] | |||
[[Category: Gao A]] | |||
[[Category: Liang DC]] | |||
[[Category: Yan XX]] | |||
Latest revision as of 13:57, 8 November 2023
Crystal structures of N-acyl homoserine lactonase AidH complexed with N-butanoyl homoserine
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