Structural highlights
Publication Abstract from PubMed
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 A resolution structure revealed deletions of interacting loops that protrude from the core beta-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.
Structural and functional characterization of a small chitin-active lytic polysaccharide monooxygenase domain of a multi-modular chitinase from Jonesia denitrificans.,Mekasha S, Forsberg Z, Dalhus B, Bacik JP, Choudhary S, Schmidt-Dannert C, Vaaje-Kolstad G, Eijsink VG FEBS Lett. 2016 Jan;590(1):34-42. doi: 10.1002/1873-3468.12025. Epub 2015 Dec 28. PMID:26763108[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mekasha S, Forsberg Z, Dalhus B, Bacik JP, Choudhary S, Schmidt-Dannert C, Vaaje-Kolstad G, Eijsink VG. Structural and functional characterization of a small chitin-active lytic polysaccharide monooxygenase domain of a multi-modular chitinase from Jonesia denitrificans. FEBS Lett. 2016 Jan;590(1):34-42. doi: 10.1002/1873-3468.12025. Epub 2015 Dec 28. PMID:26763108 doi:http://dx.doi.org/10.1002/1873-3468.12025
