9BD5

Laccase from Bacillus licheniformis

Summary for 9BD5

• Entry DOI: 10.2210/pdb9bd5/pdb
• Descriptor: Spore coat protein A, SULFATE ION, COPPER (II) ION, ... (4 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: Bacillus paralicheniformis ATCC 9945a
• Total number of polymer chains: 2
• Total formula weight: 125673.11

Authors

Habib, M.H.,Smith, T.J. (deposition date: 2024-04-11, release date: 2024-11-20, Last modification date: 2024-12-18)

Primary citation

Refaat, M.,ElRakaiby, M.T.,El Hariri El Nokab, M.,Es Sayed, J.,Elshewy, A.,Sebakhy, K.O.,Moneib, N.,Wang, T.,Smith, T.J.,Habib, M.H.
Polymerization potential of a bacterial CotA-laccase for beta-naphthol: enzyme structure and comprehensive polymer characterization.
Front Microbiol, 15:1501112-1501112, 2024

PubMed Abstract: Laccases are blue-multicopper containing enzymes that are known to play a role in the bioconversion of recalcitrant compounds. Their role in free radical polymerization of aromatic compounds for their valorization remains underexplored. In this study, we used a pBAD plasmid containing a previously characterized CotA laccase gene (abbreviated as -Lacc) from strain ATCC 9945a to express this enzyme and explore its biotransformation/polymerization potential on β-naphthol.

PubMed: 39640860
DOI: 10.3389/fmicb.2024.1501112

Experimental method

X-RAY DIFFRACTION (2.7 Å)