5VG1

Neutron crystallographic structure of a Jonesia denitrificans lytic polysaccharide monooxygenase

Summary for 5VG1

• Entry DOI: 10.2210/pdb5vg1/pdb
• Related: 5VG0
• Descriptor: Chitinase, COPPER (II) ION, PEROXIDE ION, ... (4 entities in total)
• Functional Keywords: histidine brace, hydrolase, sugar binding protein
• Biological source: Jonesia denitrificans (strain ATCC 14870 / DSM 20603 / CIP 55134)
• Total number of polymer chains: 2
• Total formula weight: 31244.88

Authors

Bacik, J.-P.,Unkefer, C.J.,Chen, J.C.H. (deposition date: 2017-04-10, release date: 2017-05-24, Last modification date: 2024-10-30)

Primary citation

Bacik, J.P.,Mekasha, S.,Forsberg, Z.,Kovalevsky, A.Y.,Vaaje-Kolstad, G.,Eijsink, V.G.H.,Nix, J.C.,Coates, L.,Cuneo, M.J.,Unkefer, C.J.,Chen, J.C.
Neutron and Atomic Resolution X-ray Structures of a Lytic Polysaccharide Monooxygenase Reveal Copper-Mediated Dioxygen Binding and Evidence for N-Terminal Deprotonation.
Biochemistry, 56:2529-2532, 2017

PubMed Abstract: 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 ND and ND, suggesting a role for the copper ion in shifting the pK of the amino terminus.

PubMed: 28481095
DOI: 10.1021/acs.biochem.7b00019

Experimental method

NEUTRON DIFFRACTION (2.1 Å)