5AA7

Structural and functional characterization of a chitin-active 15.5 kDa lytic polysaccharide monooxygenase domain from a modular chitinase from Jonesia denitrificans

Summary for 5AA7

• Entry DOI: 10.2210/pdb5aa7/pdb
• Descriptor: CHITINASE, COPPER (I) ION (3 entities in total)
• Functional Keywords: hydrolase
• Biological source: JONESIA DENITRIFICANS
• Total number of polymer chains: 2
• Total formula weight: 31212.88

Authors

Mekasha, S.,Forsberg, Z.,Dalhus, B.,Choudhary, S.,Schmidt-Dannert, C.,Vaaje-Kolstad, G.,Eijsink, V. (deposition date: 2015-07-23, release date: 2015-12-09, Last modification date: 2024-10-16)

Primary citation

Mekasha, S.,Forsberg, Z.,Dalhus, B.,Bacik, J.,Choudhary, S.,Schmidt-Dannert, C.,Vaaje-Kolstad, G.,Eijsink, V.G.H.
Structural and Functional Characterization of a Small Chitin-Active Lytic Polysaccharide Monooxygenase Domain of a Multi-Modular Chitinase from Jonesia Denitrificans.
FEBS Lett., 590:34-, 2016

PubMed 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.

PubMed: 26763108
DOI: 10.1002/1873-3468.12025

Experimental method

X-RAY DIFFRACTION (1.55 Å)