5TKG

Neurospora crassa polysaccharide monooxygenase 2 resting state

Summary for 5TKG

• Entry DOI: 10.2210/pdb5tkg/pdb
• Related: 5TKI 5TKf 5TKh
• Descriptor: Lytic polysaccharide monooxygenase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: oxidoreductase, polysaccharide monooxygenase
• Biological source: Neurospora crassa
• Total number of polymer chains: 2
• Total formula weight: 47800.24

Authors

O'Dell, W.B.,Meilleur, F. (deposition date: 2016-10-06, release date: 2017-05-17, Last modification date: 2023-10-04)

Primary citation

O'Dell, W.B.,Agarwal, P.K.,Meilleur, F.
Oxygen Activation at the Active Site of a Fungal Lytic Polysaccharide Monooxygenase.
Angew. Chem. Int. Ed. Engl., 56:767-770, 2017

PubMed Abstract: Lytic polysaccharide monooxygenases have attracted vast attention owing to their abilities to disrupt glycosidic bonds via oxidation instead of hydrolysis and to enhance enzymatic digestion of recalcitrant substrates including chitin and cellulose. We have determined high-resolution X-ray crystal structures of an enzyme from Neurospora crassa in the resting state and of a copper(II) dioxo intermediate complex formed in the absence of substrate. X-ray crystal structures also revealed "pre-bound" molecular oxygen adjacent to the active site. An examination of protonation states enabled by neutron crystallography and density functional theory calculations identified a role for a conserved histidine in promoting oxygen activation. These results provide a new structural description of oxygen activation by substrate free lytic polysaccharide monooxygenases and provide insights that can be extended to reactivity in the enzyme-substrate complex.

PubMed: 28004877
DOI: 10.1002/anie.201610502

Experimental method

X-RAY DIFFRACTION (1.2 Å)