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5MSZ

Lytic Polysaccharide Monooxygenase AA15 from Thermobia domestica in the Cu(I) State

Summary for 5MSZ
Entry DOI10.2210/pdb5msz/pdb
DescriptorThermobia domestica domestica AA15, 1,2-ETHANEDIOL, COPPER (I) ION, ... (4 entities in total)
Functional Keywordslytic polysaccharide monooxygenase, cazy, aa15, cellulose, chitin, copper, oxidoreductase
Biological sourceThermobia domestica (firebrat)
Total number of polymer chains1
Total formula weight22614.47
Authors
Primary citationSabbadin, F.,Hemsworth, G.R.,Ciano, L.,Henrissat, B.,Dupree, P.,Tryfona, T.,Marques, R.D.S.,Sweeney, S.T.,Besser, K.,Elias, L.,Pesante, G.,Li, Y.,Dowle, A.A.,Bates, R.,Gomez, L.D.,Simister, R.,Davies, G.J.,Walton, P.H.,Bruce, N.C.,McQueen-Mason, S.J.
An ancient family of lytic polysaccharide monooxygenases with roles in arthropod development and biomass digestion.
Nat Commun, 9:756-756, 2018
Cited by
PubMed Abstract: Thermobia domestica belongs to an ancient group of insects and has a remarkable ability to digest crystalline cellulose without microbial assistance. By investigating the digestive proteome of Thermobia, we have identified over 20 members of an uncharacterized family of lytic polysaccharide monooxygenases (LPMOs). We show that this LPMO family spans across several clades of the Tree of Life, is of ancient origin, and was recruited by early arthropods with possible roles in remodeling endogenous chitin scaffolds during development and metamorphosis. Based on our in-depth characterization of Thermobia's LPMOs, we propose that diversification of these enzymes toward cellulose digestion might have endowed ancestral insects with an effective biochemical apparatus for biomass degradation, allowing the early colonization of land during the Paleozoic Era. The vital role of LPMOs in modern agricultural pests and disease vectors offers new opportunities to help tackle global challenges in food security and the control of infectious diseases.
PubMed: 29472725
DOI: 10.1038/s41467-018-03142-x
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.1 Å)
Structure validation

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