title: Structural and functional characterization of a small chitin-active lytic polysaccharide monooxygenase domain of a multi-modular chitinase from Jonesia denitrificans.
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.
authors.affiliation: Department of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, Ås, Norway.
authors.forename: Sophanit
authors.initials: S
authors.lastname: Mekasha
authors.affiliation: Department of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, Ås, Norway.
authors.forename: Zarah
authors.initials: Z
authors.lastname: Forsberg
authors.affiliation: Department of Medical Biochemistry, Institute for Clinical Medicine, University of Oslo, Norway.|Department of Microbiology, Clinic for Diagnostics and Intervention, Oslo University Hospital, Rikshospitalet, Norway.
authors.forename: Bjørn
authors.initials: B
authors.lastname: Dalhus
authors.affiliation: Bioscience Division, Protein Crystallography Station, Los Alamos National Laboratory, NM, USA.
authors.forename: John-Paul
authors.initials: JP
authors.lastname: Bacik
authors.affiliation: Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, St. Paul, MN, USA.
authors.forename: Swati
authors.initials: S
authors.lastname: Choudhary
authors.affiliation: Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, St. Paul, MN, USA.
authors.forename: Claudia
authors.initials: C
authors.lastname: Schmidt-Dannert
authors.affiliation: Department of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, Ås, Norway.
authors.forename: Gustav
authors.initials: G
authors.lastname: Vaaje-Kolstad
authors.affiliation: Department of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, Ås, Norway.
authors.forename: Vincent G H
authors.initials: VG
authors.lastname: Eijsink
mesh_terms: D039903:Actinobacteria / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites; D020134:Catalytic Domain; D002482:Cellulose / Q000737:chemistry / Q000378:metabolism*; D002686:Chitin / Q000737:chemistry / Q000378:metabolism*; D002688:Chitinases / Q000737:chemistry / Q000378:metabolism*; D017124:Conserved Sequence; D018360:Crystallography, X-Ray; D006868:Hydrolysis; D006899:Mixed Function Oxygenases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D010802:Phylogeny; D011487:Protein Conformation; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D040681:Structural Homology, Protein; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D010446:Peptide Fragments; D021122:Protein Subunits; D011994:Recombinant Proteins; D002686:Chitin; D002482:Cellulose; D006899:Mixed Function Oxygenases; D002688:Chitinases
keywords: AA10; Jonesia denitrificans; chitin; chitinase; lytic polysaccharide monooxygenase