TY - JOUR
T1 - Neutron and Atomic Resolution X-ray Structures of a Lytic Polysaccharide Monooxygenase Reveal Copper-Mediated Dioxygen Binding and Evidence for N-Terminal Deprotonation
AU - Bacik, John Paul
AU - Mekasha, Sophanit
AU - Forsberg, Zarah
AU - Kovalevsky, Andrey Y.
AU - Vaaje-Kolstad, Gustav
AU - Eijsink, Vincent G.H.
AU - Nix, Jay C.
AU - Coates, Leighton
AU - Cuneo, Matthew J.
AU - Unkefer, Clifford J.
AU - Chen, Julian C.H.
N1 - Publisher Copyright:
© 2017 American Chemical Society.
PY - 2017/5/23
Y1 - 2017/5/23
N2 - A 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.
AB - A 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.
UR - http://www.scopus.com/inward/record.url?scp=85019885371&partnerID=8YFLogxK
U2 - 10.1021/acs.biochem.7b00019
DO - 10.1021/acs.biochem.7b00019
M3 - Article
C2 - 28481095
AN - SCOPUS:85019885371
SN - 0006-2960
VL - 56
SP - 2529
EP - 2532
JO - Biochemistry
JF - Biochemistry
IS - 20
ER -