Genes Identification, Molecular Docking and Dynamics Simulation Analysis of Laccases from <i>Amylostereum areolatum</i> Provides Molecular Basis of Laccase Bound to Lignin

• Main Authors: Ningning Fu, Jiaxing Li, Ming Wang, Lili Ren, Youqing Luo
• Format: Article
• Language: English
• Published: MDPI AG 2020-11-01
• Series: International Journal of Molecular Sciences
• Subjects: <i>Amylostereum areolatum</i>; <i>Sirex noctilio</i>; laccases; molecular docking and dynamics simulation; protein-ligand interaction
• Online Access: https://www.mdpi.com/1422-0067/21/22/8845

An obligate mutualistic relationship exists between the fungus<i> Amylostereum areolatum</i> and woodwasp<i> Sirex noctilio</i>. The fungus digests lignin in the host pine, providing essential nutrients for the growing woodwasp larvae. However, the functional properties of this symbiosis are poorly described. In this study, we identified, cloned, and characterized 14 laccase genes from <i>A. areolatum</i>. These genes encoded proteins of 508 to 529 amino acids and contained three typical copper-oxidase domains, necessary to confer laccase activity. Besides, we performed molecular docking and dynamics simulation of the laccase proteins in complex with lignin compounds (monomers, dimers, trimers, and tetramers). AaLac2, AaLac3, AaLac6, AaLac8, and AaLac10 were found that had low binding energies with all lignin model compounds tested and three of them could maintain stability when binding to these compounds. Among these complexes, amino acid residues ALA, GLN, LEU, PHE, PRO, and SER were commonly present. Our study reveals the molecular basis of <i>A. areolatum</i> laccases interacting with lignin, which is essential for understanding how the fungus provides nutrients to <i>S. noctilio.</i> These findings might also provide guidance for the control of <i>S. noctilio</i> by informing the design of enzyme mutants that could reduce the efficiency of lignin degradation.