This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4yf9

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Structure of N-acylhomoserine lactone acylase MacQ

Structural highlights

4yf9 is a 12 chain structure with sequence from Acidovorax sp. MR-S7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A0A1VBK6_9BURK

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4yf9"

Categories: Acidovorax sp. MR-S7 | Large Structures | Kimura N | Kusada H | Yasutake Y

@@ Line 3: / Line 3: @@
 <StructureSection load='4yf9' size='340' side='right'caption='[[4yf9]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4yf9]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YF9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YF9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4yf9]] 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=4YF9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YF9 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yfa|4yfa]], [[4yfb|4yfb]]</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]] 2.6&#8491;</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=4yf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yf9 OCA], [http://pdbe.org/4yf9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yf9 RCSB], [http://www.ebi.ac.uk/pdbsum/4yf9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yf9 ProSAT]</span></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=4yf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yf9 OCA], [https://pdbe.org/4yf9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yf9 RCSB], [https://www.ebi.ac.uk/pdbsum/4yf9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yf9 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/A0A0A1VBK6_9BURK A0A0A1VBK6_9BURK]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 22: @@
 __TOC__
 </StructureSection>
+[[Category: Acidovorax sp. MR-S7]]
 [[Category: Large Structures]]
-[[Category: Kimura, N]]
+[[Category: Kimura N]]
-[[Category: Kusada, H]]
+[[Category: Kusada H]]
-[[Category: Yasutake, Y]]
+[[Category: Yasutake Y]]
-[[Category: Acylase]]
-[[Category: Hydrolase]]
-[[Category: Ntn-hydrolase fold]]

4yf9

From Proteopedia

Current revision

Structure of N-acylhomoserine lactone acylase MacQ

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox