4MAH

Structure of Aspergillus oryzae AA11 Lytic Polysaccharide Monooxygenase with Zn

Summary for 4MAH

• Entry DOI: 10.2210/pdb4mah/pdb
• Related: 4MAI
• Descriptor: AA11 Lytic Polysaccharide Monooxygenase, ZINC ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• Functional Keywords: chitin oxidation, gh61, aa11, chitin degradation, oxidoreductase
• Biological source: Aspergillus oryzae (Yellow koji mold)
• Total number of polymer chains: 1
• Total formula weight: 23240.77

Authors

Hemsworth, G.R.,Henrissat, B.,Walton, P.H.,Davies, G.J. (deposition date: 2013-08-16, release date: 2013-12-18, Last modification date: 2017-11-15)

Primary citation

Hemsworth, G.R.,Henrissat, B.,Davies, G.J.,Walton, P.H.
Discovery and characterization of a new family of lytic polysaccharide monooxygenases.
Nat.Chem.Biol., 10:122-126, 2014

PubMed Abstract: Lytic polysaccharide monooxygenases (LPMOs) are a recently discovered class of enzymes capable of oxidizing recalcitrant polysaccharides. They are attracting considerable attention owing to their potential use in biomass conversion, notably in the production of biofuels. Previous studies have identified two discrete sequence-based families of these enzymes termed AA9 (formerly GH61) and AA10 (formerly CBM33). Here, we report the discovery of a third family of LPMOs. Using a chitin-degrading exemplar from Aspergillus oryzae, we show that the three-dimensional structure of the enzyme shares some features of the previous two classes of LPMOs, including a copper active center featuring the 'histidine brace' active site, but is distinct in terms of its active site details and its EPR spectroscopy. The newly characterized AA11 family expands the LPMO clan, potentially broadening both the range of potential substrates and the types of reactive copper-oxygen species formed at the active site of LPMOs.

PubMed: 24362702
DOI: 10.1038/nchembio.1417

Experimental method

X-RAY DIFFRACTION (1.55 Å)