Journal
CARBOHYDRATE RESEARCH
Volume 448, Issue -, Pages 187-190Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.carres.2017.03.010
Keywords
Lytic polysaccharide monooxygenases; Cellohexaose interactions; pH-dependent disorder
Funding
- Danish Council for Strategic Research through the ERAIB program funding [12-134923]
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Lytic polysaccharide monooxygenases (LPMOs) have been found to be key components in microbial (bacterial and fungal) degradation of biomass. They are copper metalloenzymes that degrade polysaccharides oxidatively and act in synergy with glycoside hydrolases. Recently crystallographic studies carried out at pH 5.5 of the LPMO from Lentinus similis belonging to the fungal LPMO family AA9 have provided the first atomic resolution view of substrate-LPMO interactions. The LsAA9A structure presented here determined at pH 3.5 shows significant disorder of the active site in the absence of substrate ligand. Furthermore some differences are also observed in regards to substrate (cellohexaose) binding, although the major interaction with the N-terminal histidine remains unchanged. (C) 2017 Elsevier Ltd. All rights reserved.
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