Abstract
Lytic polysaccharide monooxygenases (LPMOs) are copper metalloenzymes which cleave polysaccharides oxidatively and are important in pathogen biology, carbon cycling and biotechnology. The Lentinus similis family AA9 isoform A (LsAA9_A) has been extensively studied as a model system because its activity towards smaller soluble saccharide substrates has allowed detailed structural characterization of its interaction with a variety of substrates by X-ray crystallography at high resolution. Here, the joint X-ray/neutron room-temperature crystallographic structure of carbohydrate-free LsAA9_A in the copper(II) resting state refined against X-ray and neutron data at 2.1 and 2.8 Å resolution, respectively, is presented. The results provide an experimental determination of the protonation states of the copper(II)-coordinating residues and second-shell residues in LsAA9_A, paving the way for future neutron crystallographic studies of LPMO-carbohydrate complexes.
| Original language | English |
|---|---|
| Journal | Acta crystallographica. Section F, Structural biology communications |
| Volume | 79 |
| Issue number | 1 |
| Pages (from-to) | 1-7 |
| Number of pages | 7 |
| ISSN | 2053-230X |
| DOIs | |
| Publication status | Published - 2023 |
Bibliographical note
Publisher Copyright:open access.
Keywords
- copper metalloenzymes
- Lentinus similis AA9_A
- lytic polysaccharide monooxygenases
- neutron crystallography
- protonation states
Cite this
- APA
- Standard
- Harvard
- Vancouver
- Author
- BIBTEX
- RIS