Structural and functional characterization of a small chitin-active lytic polysaccharide monooxygenase domain of a multi-modular chitinase from Jonesia denitrificans

FEBS Letters
Sophanit MekashaVincent G H Eijsink

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.

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Citations

Mar 16, 2017·Carbohydrate Research·Gaston CourtadeFinn L Aachmann
Jul 1, 2017·Microbiology and Molecular Biology Reviews : MMBR·Marco AgostoniMichael A Marletta
May 14, 2020·The Journal of Biological Chemistry·Sophanit MekashaVincent G H Eijsink
Jan 7, 2019·Journal of Molecular Graphics & Modelling·Radhika AroraRagothaman M Yennamalli
Nov 6, 2020·Journal of Agricultural and Food Chemistry·Yuko S NakagawaGustav Vaaje-Kolstad

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