7ALZ

GqqA- a novel type of quorum quenching acylases

Summary for 7ALZ

• Entry DOI: 10.2210/pdb7alz/pdb
• Descriptor: Prephenate dehydratase, PHENYLALANINE (3 entities in total)
• Functional Keywords: quorum quenching, acylase, hydrolase
• Biological source: Komagataeibacter europaeus
• Total number of polymer chains: 2
• Total formula weight: 62172.39

Authors

Werner, N.,Betzel, C. (deposition date: 2020-10-07, release date: 2021-08-04, Last modification date: 2024-10-16)

Primary citation

Werner, N.,Petersen, K.,Vollstedt, C.,Garcia, P.P.,Chow, J.,Ferrer, M.,Fernandez-Lopez, L.,Falke, S.,Perbandt, M.,Hinrichs, W.,Betzel, C.,Streit, W.R.
The Komagataeibacter europaeus GqqA is the prototype of a novel bifunctional N-Acyl-homoserine lactone acylase with prephenate dehydratase activity.
Sci Rep, 11:12255-12255, 2021

PubMed Abstract: Previously, we reported the isolation of a quorum quenching protein (QQ), designated GqqA, from Komagataeibacter europaeus CECT 8546 that is highly homologous to prephenate dehydratases (PDT) (Valera et al. in Microb Cell Fact 15, 88. https://doi.org/10.1186/s12934-016-0482-y , 2016). GqqA strongly interfered with N-acyl-homoserine lactone (AHL) quorum sensing signals from Gram-negative bacteria and affected biofilm formation in its native host strain Komagataeibacter europaeus. Here we present and discuss data identifying GqqA as a novel acylase. ESI-MS-MS data showed unambiguously that GqqA hydrolyzes the amide bond of the acyl side-chain of AHL molecules, but not the lactone ring. Consistent with this observation the protein sequence does not carry a conserved Zn binding motif, known to be essential for metal-dependent lactonases, but in fact harboring the typical periplasmatic binding protein domain (PBP domain), acting as catalytic domain. We report structural details for the native structure at 2.5 Å resolution and for a truncated GqqA structure at 1.7 Å. The structures obtained highlight that GqqA acts as a dimer and complementary docking studies indicate that the lactone ring of the substrate binds within a cleft of the PBP domain and interacts with polar residues Y16, S17 and T174. The biochemical and phylogenetic analyses imply that GqqA represents the first member of a novel type of QQ family enzymes.

PubMed: 34112823
DOI: 10.1038/s41598-021-91536-1

Experimental method

X-RAY DIFFRACTION (1.67 Å)