Abstract
Lytic polysaccharide monooxygenases (LPMOs) boost enzymatic depolymerization of recalcitrant polysaccharides, such as chitin and cellulose. We have studied a chitin-active LPMO domain (JdLPMO10A) that is considerably smaller (15.5 kDa) than all structurally characterized LPMOs so far and that is part of a modular protein containing a GH18 chitinase. The 1.55 Å resolution structure revealed deletions of interacting loops that protrude from the core β-sandwich scaffold in larger LPMO10s. Despite these deletions, the enzyme is active on alpha- and beta-chitin, and the chitin-binding surface previously described for larger LPMOs is fully conserved. JdLPMO10A may represent a minimal scaffold needed to catalyse the powerful LPMO reaction.
Keywords:
AA10; Jonesia denitrificans; chitin; chitinase; lytic polysaccharide monooxygenase.
© 2015 Federation of European Biochemical Societies.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Actinobacteria / enzymology*
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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Binding Sites
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Catalytic Domain
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Cellulose / chemistry
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Cellulose / metabolism*
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Chitin / chemistry
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Chitin / metabolism*
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Chitinases / chemistry
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Chitinases / metabolism*
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Conserved Sequence
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Crystallography, X-Ray
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Hydrolysis
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Mixed Function Oxygenases / chemistry
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Mixed Function Oxygenases / genetics
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Mixed Function Oxygenases / metabolism*
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Models, Molecular*
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Molecular Weight
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Peptide Fragments / chemistry
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Peptide Fragments / genetics
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Peptide Fragments / metabolism
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Phylogeny
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Protein Conformation
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Protein Subunits / chemistry
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Protein Subunits / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Structural Homology, Protein
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Substrate Specificity
Substances
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Bacterial Proteins
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Peptide Fragments
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Protein Subunits
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Recombinant Proteins
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Chitin
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Cellulose
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Mixed Function Oxygenases
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Chitinases