Structural studies of Neurospora crassa LPMO9D and redox partner CDHIIA using neutron crystallography and small-angle scattering

Bodenheimer, Annette M.; O'Dell, William B.; Stanley, Christopher B.; Meilleur, Flora

doi:10.1016/j.carres.2017.03.001

Structural studies of Neurospora crassa LPMO9D and redox partner CDHIIA using neutron crystallography and small-angle scattering

Journal Article · Sat Mar 04 00:00:00 UTC 2017 · Carbohydrate Research

DOI:https://doi.org/10.1016/j.carres.2017.03.001· OSTI ID:1424447

Bodenheimer, Annette M. ^[1]; ^[1]; Stanley, Christopher B. ^[2]; Meilleur, Flora ^[1]

North Carolina State Univ., Raleigh, NC (United States). Dept. of Molecular and Structural Biochemistry; Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Neutron Sciences Directorate
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Neutron Sciences Directorate

Sensitivity to hydrogen/deuterium and lack of observable radiation damage makes cold neutrons an ideal probe the structural studies of proteins with highly photosensitive groups such as the copper center of lytic polysaccharide monooxygenases (LPMOs) and flavin adenine dinucleotide (FAD) and heme redox cofactors of cellobiose dehydrogenases (CDHs). In this paper, neutron crystallography and small-angle neutron scattering are used to investigate Neurospora crassa LPMO9D (NcLPMO9D) and CDHIIA (NcCDHIIA), respectively. The presence of LPMO greatly enhances the efficiency of commercial glycoside hydrolase cocktails in the depolymerization of cellulose. LPMOs can receive electrons from CDHs to activate molecular dioxygen for the oxidation of cellulose resulting in chain cleavage and disruption of local crystallinity. Using neutron protein crystallography, the hydrogen/deuterium atoms of NcLPMO9D could be located throughout the structure. At the copper active site, the protonation states of the side chains of His1, His84, His157 and Tyr168, and the orientation of water molecules could be determined. Small-angle neutron scattering measurements provided low resolution models of NcCDHIIA with both the dehydrogenase and cytochrome domains in oxidized states that exhibited elongated conformations. Finally, this work demonstrates the suitability of neutron diffraction and scattering for characterizing enzymes critical to oxidative cellulose deconstruction.

View Accepted Manuscript (DOE)

Research Organization:: North Carolina State Univ., Raleigh, NC (United States); Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)

Sponsoring Organization:: National Science Foundation (NSF) (United States); USDA National Inst. of Food and Agriculture (NIFA); USDOE Office of Science (SC), Basic Energy Sciences (BES); USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22); USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)

Grant/Contract Number:: AC05-00OR22725

OSTI ID:: 1424447

Alternate ID(s):: OSTI ID: 1576621

Journal Information:: Carbohydrate Research, Journal Name: Carbohydrate Research Vol. 448; ISSN 0008-6215

Country of Publication:: United States

Language:: English

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