Neutron and high-resolution room-temperature X-ray data collection from crystallized lytic polysaccharide monooxygenase
- Los Alamos National Lab. (LANL), Los Alamos, NM (United States)
- Norwegian Univ. of Life Sciences (Norway)
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
- Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Bacteria and fungi express lytic polysaccharide monooxgyenase (LPMO) enzymes that act in conjunction with canonical hydrolytic sugar-processing enzymes to rapidly convert polysaccharides such as chitin, cellulose and starch to single monosaccharide products. In order to gain a better understanding of the structure and oxidative mechanism of these enzymes, large crystals (1–3 mm3) of a chitin-processing LPMO from the Gram-positive soil bacterium Jonesia denitrificans were grown and screened for their ability to diffract neutrons. In addition to the collection of neutron diffraction data, which were processed to 2.1 Å resolution, a high-resolution room-temperature X-ray diffraction data set was collected and processed to 1.1 Å resolution in space group P212121. To our knowledge, this work marks the first successful neutron crystallographic experiment on an LPMO. As a result, joint X-ray/neutron refinement of the resulting data will reveal new details of the structure and mechanism of this recently discovered class of enzymes.
- Research Organization:
- Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Spallation Neutron Source (SNS)
- Sponsoring Organization:
- USDOE
- Grant/Contract Number:
- AC05-00OR22725
- OSTI ID:
- 1334453
- Journal Information:
- Acta Crystallographica. Section F, Structural Biology Communications, Vol. 71, Issue 11; ISSN 2053-230X
- Publisher:
- International Union of CrystallographyCopyright Statement
- Country of Publication:
- United States
- Language:
- English
Web of Science
Detection and Characterization of a Novel Copper‐Dependent Intermediate in a Lytic Polysaccharide Monooxygenase
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journal | November 2019 |
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