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Neutron and Atomic Resolution X‑ray Structures of a Lytic Polysaccharide Monooxygenase Reveal Copper-Mediated Dioxygen Binding and Evidence for N‑Terminal Deprotonation
journal contribution
posted on 2017-05-08, 00:00 authored by John-Paul Bacik, Sophanit Mekasha, Zarah Forsberg, Andrey Y. Kovalevsky, Gustav Vaaje-Kolstad, Vincent G. H. Eijsink, Jay C. Nix, Leighton Coates, Matthew J. Cuneo, Clifford J. Unkefer, Julian C.-H. ChenA 1.1
Å resolution, room-temperature X-ray structure and a
2.1 Å resolution neutron structure of a chitin-degrading lytic
polysaccharide monooxygenase domain from the bacterium Jonesia
denitrificans (JdLPMO10A) show a putative
dioxygen species equatorially bound to the active site copper. Both
structures show an elongated density for the dioxygen, most consistent
with a Cu(II)-bound peroxide. The coordination environment is consistent
with Cu(II). In the neutron and X-ray structures, difference maps
reveal the N-terminal amino group, involved in copper coordination,
is present as a mixed ND2 and ND–, suggesting
a role for the copper ion in shifting the pKa of the amino terminus.
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copper ionroom-temperature X-ray structurecopper coordinationp Kstructures showLytic Polysaccharide Monooxygenase Reveal Copper-Mediated Dioxygen BindingJd LPMO 10A showdioxygen species equatoriallysite copperbacterium Jonesia denitrificansND 2difference mapschitin-degrading lytic polysaccharide monooxygenase domaincoordination environmentX-ray structures2.1 Å resolution neutron structure1.1 Å resolutionCu
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