View source for 4yfa


==Structure of N-acylhomoserine lactone acylase MacQ in complex with decanoic acid==
<StructureSection load='4yfa' size='340' side='right'caption='[[4yfa]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4yfa]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidovorax_sp._MR-S7 Acidovorax sp. MR-S7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YFA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YFA 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DKA:DECANOIC+ACID'>DKA</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=4yfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yfa OCA], [https://pdbe.org/4yfa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yfa RCSB], [https://www.ebi.ac.uk/pdbsum/4yfa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yfa ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0A1VBK6_9BURK A0A0A1VBK6_9BURK] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Understanding the molecular mechanisms of bacterial antibiotic resistance will help prepare against further emergence of multi-drug resistant strains. MacQ is an enzyme responsible for the multi-drug resistance of Acidovorax sp. strain MR-S7. MacQ has acylase activity against both N-acylhomoserine lactones (AHLs), a class of signalling compounds involved in quorum sensing, and beta-lactam antibiotics. Thus, MacQ is crucial as a quencher of quorum sensing as well as in conferring antibiotic resistance in Acidovorax. Here, we report the X-ray structures of MacQ in ligand-free and reaction product complexes. MacQ forms a 170-kDa capsule-shaped molecule via face-to-face interaction with two heterodimers consisting of an alpha-chain and a beta-chain, generated by the self-cleaving activity of a precursor polypeptide. The electron density of the spacer polypeptide in the hollow of the molecule revealed the close orientation of the peptide-bond atoms of Val20SP-Gly21SP to the active-site, implying a role of the residues in substrate binding. In mutational analyses, uncleaved MacQ retained degradation activity against both AHLs and penicillin G. These results provide novel insights into the mechanism of self-cleaving maturation and enzymatic function of N-terminal nucleophile hydrolases.

Bifunctional quorum-quenching and antibiotic-acylase MacQ forms a 170-kDa capsule-shaped molecule containing spacer polypeptides.,Yasutake Y, Kusada H, Ebuchi T, Hanada S, Kamagata Y, Tamura T, Kimura N Sci Rep. 2017 Aug 21;7(1):8946. doi: 10.1038/s41598-017-09399-4. PMID:28827579<ref>PMID:28827579</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4yfa" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Acidovorax sp. MR-S7]]
[[Category: Large Structures]]
[[Category: Kimura N]]
[[Category: Kusada H]]
[[Category: Yasutake Y]]