Crystal structure of VmoLac, a tentative quorum quenching lactonase from the extremophilic crenarchaeon Vulcanisaeta moutnovskia

Scientific Reports

Volumn 5, Issue , 2015, Pages 8372-

  Hiblot, Julien ^a,c   Bzdrenga, Janek ^a   Champion, Charlotte ^a   Chabriere, Eric ^a   Elias, Mikael ^b  

^a AIX MARSEILLE UNIVERSITY   (France)

^b UNIVERSITY OF MINNESOTA   (United States)

^c EPFL   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

ARCHAEAL PROTEIN; GAMMA BUTYROLACTONE DERIVATIVE; PHOSPHOTRIESTERASE;

ARCHAEON; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; X RAY CRYSTALLOGRAPHY;

ACYL-BUTYROLACTONES; ARCHAEA; ARCHAEAL PROTEINS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; PHOSPHORIC TRIESTER HYDROLASES;

EID: 84923040457     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep08372     Document Type: Article

References (43)

1. Afriat, L., Roodveldt, C., Manco, G. & Tawfik, D. S. The latent promiscuity of newly identified microbial lactonases is linked to a recently diverged phosphotriesterase. Biochemistry 45, 13677-86 (2006).
2. Merone, L., Mandrich, L., Rossi, M. & Manco, G. A thermostable phosphotriesterase from the archaeon Sulfolobus solfataricus: cloning, overexpression and properties. Extremophiles 9, 297-305 (2005).
3. Hawwa, R., Larsen, S. D., Ratia, K. &Mesecar, A. D. Structure-based and random mutagenesis approaches increase the organophosphate-degrading activity of a phosphotriesterase homologue from Deinococcus radiodurans. J Mol Biol 393, 36-57 (2009).
4. Hiblot, J., Gotthard, G., Chabriere, E. & Elias, M. Characterisation of the organophosphate hydrolase catalytic activity of SsoPox. Sci. Rep. 2, 779; DOI:10.1038/srep00779 (2012).
5. Omburo, G. A., Kuo, J. M.,Mullins, L. S. & Raushel, F. M. Characterization of the zinc binding site of bacterial phosphotriesterase. J Biol Chem 267, 13278-83 (1992).
6. Elias, M. & Tawfik, D. S. Divergence and Convergence in Enzyme Evolution: Parallel Evolution of Paraoxonases from Quorum-quenching Lactonases. J Biol Chem 287, 11-20 (2012).
7. Hiblot, J., Gotthard, G., Elias, M. & Chabriere, E. Differential Active Site Loop Conformations Mediate Promiscuous Activities in the Lactonase Pox. PLoS One 8, e75272 (2013).
8. Hiblot, J., Gotthard, G., Chabriere, E. & Elias, M. Structural and Enzymatic characterization of the lactonase SisLac from Sulfolobus islandicus . PLoS One 7, e47028 (2012).
9. Xiang, D. F. et al. Functional annotation and three-dimensional structure of Dr0930 from Deinococcus radiodurans, a close relative of phosphotriesterase in the amidohydrolase superfamily. Biochemistry 48, 2237-47 (2009).
10. Hawwa, R., Aikens, J., Turner, R. J., Santarsiero, B. D. &Mesecar, A. D. Structural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilus. Arch Biochem Biophys 488, 109-20 (2009).
11. Dong, Y. H. et al. Quenching quorum-sensing-dependent bacterial infection by an N-acyl homoserine lactonase. Nature 411, 813-7 (2001).
12. Amara, N., Krom, B. P., Kaufmann, G. F. & Meijler, M. M. Macromolecular inhibition of quorum sensing: enzymes, antibodies, and beyond. Chem Rev 111, 195-208 (2011).
13. Koch, G. et al. Reducing virulence of the human pathogen Burkholderia by altering the substrate specificity of the quorum-quenching acylase PvdQ. Proc Natl Acad Sci U S A 111, 1568-1573 (2014).
14. Dong, Y. H., Xu, J. L., Li, X. Z. & Zhang, L. H. AiiA, an enzyme that inactivates the acylhomoserine lactone quorum-sensing signal and attenuates the virulence of Erwinia carotovora. Proc Natl Acad Sci U S A 97, 3526-31 (2000).
15. Augustine, N., Kumar, P. & Thomas, S. Inhibition of Vibrio cholerae biofilm by AiiA enzyme produced from Bacillus spp. Arch Microbiol 192, 1019-1022 (2010).
16. Seibert, C. M. & Raushel, F. M. Structural and catalytic diversity within the amidohydrolase superfamily. Biochemistry 44, 6383-91 (2005).
17. Elias, M. et al. Structural basis for natural lactonase and promiscuous phosphotriesterase activities. J Mol Biol 379, 1017-28 (2008).
18. Del Vecchio, P. et al. Structural determinants of the high thermal stability of SsoPox from the hyperthermophilic archaeon Sulfolobus solfataricus. Extremophiles 13, 461-70 (2009).
19. Jackson, C. J. et al. Conformational sampling, catalysis, and evolution of the bacterial phosphotriesterase. Proc Natl Acad Sci U S A 106, 21631-6 (2009).
20. Afriat-Jurnou, L., Jackson, C. J. & Tawfik, D. S. Reconstructing a missing link in the evolution of a recently diverged phosphotriesterase by active-site loop remodeling. Biochemistry 51, 6047-55 (2012).
21. Poirot, O.,OToole, E.&Notredame, C. Tcoffee@igs: A web server for computing, evaluating and combining multiple sequence alignments. Nucleic Acids Res 31, 3503-6 (2003).
22. Notredame, C.,Higgins, D. G. &Heringa, J. T-Coffee: A novel method for fast and accurate multiple sequence alignment. J Mol Biol 302, 205-17 (2000).
23. Gouy, M., Guindon, S. & Gascuel, O. SeaView version 4: A multiplatform graphical user interface for sequence alignment and phylogenetic tree building. Mol Biol Evol 27, 221-4 (2010).
24. Larkin,M. A. et al. Clustal W and Clustal X version 2.0. Bioinformatics 23, 2947-8 (2007).
25. van den Berg, S., Lofdahl, P. A., Hard, T. & Berglund, H. Improved solubility of TEV protease by directed evolution. J Biotechnol 121, 291-8 (2006).
26. Gotthard, G., Hiblot, J., Gonzalez, D., Elias, M. & Chabriere, E. Structural and enzymatic characterization of the phosphotriesterase OPHC2 from Pseudomonas pseudoalcaligenes. PLoS One 8, e77995 (2013).
27. Wilkins, M. R. et al. Protein identification and analysis tools in the ExPASy server. Methods Mol Biol 112, 531-52 (1999).
28. Gotthard, G., Hiblot, J., Gonzalez, D., Chabriere, E. &Elias, M. Crystallization and preliminary X-ray diffraction analysis of the organophosphorus hydrolase OPHC2 from Pseudomonas pseudoalcaligenes. Acta Crystallogr Sect F Struct Biol Cryst Commun 69, 73-6 (2013).
29. Kabsch, W. Xds. Acta Crystallogr D Biol Crystallogr 66, 125-32 (2010).
30. Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr D Biol Crystallogr 66, 486-501 (2010).
31. Murshudov, G. N. et al. REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr D Biol Crystallogr 67, 355-67 (2011).
32. Krissinel, E. & Henrick, K. Inference of macromolecular assemblies from crystalline state. J Mol Biol 372, 774-97 (2007).
33. Gumerov, V. M. et al. Complete genome sequence of "Vulcanisaeta moutnovskia" strain 768-28, a novel member of the hyperthermophilic crenarchaeal genus Vulcanisaeta. J Bacteriol 193, 2355-6 (2011).
34. Kallnik, V. et al. Characterization of a phosphotriesterase-like lactonase from the hyperthermoacidophilic crenarchaeon Vulcanisaeta moutnovskia. J Biotechnol 190, 11-17 (2014).
35. Jackson, C. J., Liu, J. W., Coote, M. L. & Ollis, D. L. The effects of substrate orientation on the mechanism of a phosphotriesterase. Org Biomol Chem 3, 4343-50 (2005).
36. Chow, J. Y. et al. Directed evolution of a thermostable quorum-quenching lactonase from the amidohydrolase superfamily. J Biol Chem 285, 40911-20 (2010).
37. Hiblot, J., Gotthard, G., Elias, M. & Chabriere, E. Differential active site loop conformationsmediate promiscuous activities in the lactonase SsoPox. PLoS One 8, e75272 (2013).
38. Hiblot, J., Gotthard, G., Champion, C., Chabriere, E. & Elias, M. Crystallization and preliminary X-ray diffraction analysis of the lactonase VmoLac from Vulcanisaeta moutnovskia. Acta Crystallogr Sect F Struct Biol Cryst Commun 69, 1235-8 (2013).
39. Vieille, C. & Zeikus, G. J. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 65, 1-43 (2001).
40. Bzdrenga, J. et al. SacPox from the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius is a proficient lactonase. BMC Res Notes 7, 333 (2014).
41. Xue, B. et al. Correction to Structural Evidence of a Productive Active Site Architecture for an Evolved Quorum-quenching GKL Lactonase. Biochemistry 51, 10120 (2012).
42. Momb, J. et al. Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 2. Substrate modeling and active site mutations. Biochemistry 47, 7715-25 (2008).
43. Liu, D. et al.Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures. Biochemistry 47, 7706-14 (2008).