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Title Role and structure of the small subunit forming heterodimers with laccase-like enzymes
ID_Doc 15322
Authors Aza, P; Linde, D; Molpeceres, G; Vind, J; Medrano, FJ; Camarero, S
Title Role and structure of the small subunit forming heterodimers with laccase-like enzymes
Year 2023
Published Protein Science, 32, 9
DOI 10.1002/pro.4734
Abstract Unlike laccases sensu stricto, which are usually monomeric enzymes, laccase-like enzymes recently re-classified as Novel Laccases (NLACs) are characterized by the formation of heterodimers with small proteins (subunits) of unknown function. Here the NLAC from Pleurotus eryngii (PeNL) and a small protein selected from the fungal genome, that is homologous to reported POXA3 from Pleurotus ostreatus, were produced in Aspergillus oryzae separately or together. The two proteins interacted regardless of whether the small subunit was co-expressed or exogenously added to the enzyme. The stability and catalytic activity of PeNL was significantly enhanced in the presence of the small subunit. Size exclusion chromatography-multi angle light scattering (SEC-MALS) analysis confirmed that the complex PeNL-ss is a heterodimer of 77.4 kDa. The crystallographic structure of the small protein expressed in Escherichia coli was solved at 1.6 & ANGS; resolution. This is the first structure elucidated of a small subunit of a NLAC. The helix bundle structure of the small subunit accommodates well with the enzyme model structure, including interactions with specific regions of NLACs and some amino acid residues of the substrate-binding loops.
Author Keywords crystal structure; heterodimer; novel laccase; Pleurotus eryngii; small subunit
Index Keywords Index Keywords
Document Type Other
Open Access Open Access
Source Science Citation Index Expanded (SCI-EXPANDED)
EID WOS:001052478600001
WoS Category Biochemistry & Molecular Biology
Research Area Biochemistry & Molecular Biology
PDF https://doi.org/10.1002/pro.4734
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