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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 69 82-91 (2013)
Related entries: 4g5x, 4g8b, 4g8d, 4g9e, 4g9g

Cited: 12 times
EuropePMC logo PMID: 23275166

Abstract

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.

Articles - 4g8c mentioned but not cited (1)

  1. 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 69 82-91 (2013)


Reviews citing this publication (4)

  1. Quorum quenching: role in nature and applied developments. Grandclément C, Tannières M, Moréra S, Dessaux Y, Faure D. FEMS Microbiol Rev 40 86-116 (2016)
  2. Bacterial Biofilm Inhibition: A Focused Review on Recent Therapeutic Strategies for Combating the Biofilm Mediated Infections. Srinivasan R, Santhakumari S, Poonguzhali P, Geetha M, Dyavaiah M, Xiangmin L. Front Microbiol 12 676458 (2021)
  3. Quorum quenching enzymes and their effects on virulence, biofilm, and microbiomes: a review of recent advances. Sikdar R, Elias M. Expert Rev Anti Infect Ther 18 1221-1233 (2020)
  4. Marine Microbiological Enzymes: Studies with Multiple Strategies and Prospects. Wang Y, Song Q, Zhang XH. Mar Drugs 14 E171 (2016)

Articles citing this publication (7)

  1. How the Same Core Catalytic Machinery Catalyzes 17 Different Reactions: the Serine-Histidine-Aspartate Catalytic Triad of α/β-Hydrolase Fold Enzymes. Rauwerdink A, Kazlauskas RJ. ACS Catal 5 6153-6176 (2015)
  2. Attenuation of Quorum Sensing Regulated Virulence of Pectobacterium carotovorum subsp. carotovorum through an AHL Lactonase Produced by Lysinibacillus sp. Gs50. Garge SS, Nerurkar AS. PLoS One 11 e0167344 (2016)
  3. Fast, Continuous, and High-Throughput (Bio)Chemical Activity Assay for N-Acyl-l-Homoserine Lactone Quorum-Quenching Enzymes. Last D, Krüger GH, Dörr M, Bornscheuer UT. Appl Environ Microbiol 82 4145-4154 (2016)
  4. Identification of a Second Type of AHL-lactonase from Rhodococcus sp. BH4, belonging to the α/β Hydrolase Superfamily. Ryu DH, Lee SW, Mikolaityte V, Kim YW, Jeong HY, Lee SJ, Lee CH, Lee JK. J Microbiol Biotechnol 30 937-945 (2020)
  5. Engineering of a thermostable esterase Est816 to improve its quorum-quenching activity and the underlying structural basis. Liu X, Cao LC, Fan XJ, Liu YH, Xie W. Sci Rep 6 38137 (2016)
  6. Targeting Multidrug-Recalcitrant Pseudomonas aeruginosa Biofilms: Combined-Enzyme Treatment Enhances Antibiotic Efficacy. Zhang Y, Wei W, Wen H, Cheng Z, Mi Z, Zhang J, Liu X, Fan X. Antimicrob Agents Chemother 67 e0135822 (2023)
  7. Improving the production of AHL lactonase AiiO-AIO6 from Ochrobactrum sp. M231 in intracellular protease-deficient Bacillus subtilis. Xia R, Yang Y, Pan X, Gao C, Yao Y, Liu X, Teame T, Zhang F, Hu J, Ran C, Zhang Z, Liu-Clarke J, Zhou Z. AMB Express 10 138 (2020)


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