5NO7
Crystal Structure of a Xylan-active Lytic Polysaccharide Monooxygenase from Pycnoporus coccineus.
Summary for 5NO7
| Entry DOI | 10.2210/pdb5no7/pdb |
| Descriptor | Lytic polysaccharide monooxygenase, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total) |
| Functional Keywords | xylan, lpmo, cellulose, oxydative enzyme, wood, oxidoreductase |
| Biological source | Pycnoporus cinnabarinus |
| Total number of polymer chains | 2 |
| Total formula weight | 74772.36 |
| Authors | Ladeveze, S.,Couturier, M.,Sulzenbacher, G.,Berrin, J.-G. (deposition date: 2017-04-11, release date: 2018-01-17, Last modification date: 2024-11-20) |
| Primary citation | Couturier, M.,Ladeveze, S.,Sulzenbacher, G.,Ciano, L.,Fanuel, M.,Moreau, C.,Villares, A.,Cathala, B.,Chaspoul, F.,Frandsen, K.E.,Labourel, A.,Herpoel-Gimbert, I.,Grisel, S.,Haon, M.,Lenfant, N.,Rogniaux, H.,Ropartz, D.,Davies, G.J.,Rosso, M.N.,Walton, P.H.,Henrissat, B.,Berrin, J.G. Lytic xylan oxidases from wood-decay fungi unlock biomass degradation. Nat. Chem. Biol., 14:306-310, 2018 Cited by PubMed Abstract: Wood biomass is the most abundant feedstock envisioned for the development of modern biorefineries. However, the cost-effective conversion of this form of biomass into commodity products is limited by its resistance to enzymatic degradation. Here we describe a new family of fungal lytic polysaccharide monooxygenases (LPMOs) prevalent among white-rot and brown-rot basidiomycetes that is active on xylans-a recalcitrant polysaccharide abundant in wood biomass. Two AA14 LPMO members from the white-rot fungus Pycnoporus coccineus substantially increase the efficiency of wood saccharification through oxidative cleavage of highly refractory xylan-coated cellulose fibers. The discovery of this unique enzyme activity advances our knowledge on the degradation of woody biomass in nature and offers an innovative solution for improving enzyme cocktails for biorefinery applications. PubMed: 29377002DOI: 10.1038/nchembio.2558 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.01 Å) |
Structure validation
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