Joint X-ray/neutron structure of Lentinus similis AA9_A at room temperature
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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.
Originalsprog | Engelsk |
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Tidsskrift | Acta crystallographica. Section F, Structural biology communications |
Vol/bind | 79 |
Udgave nummer | 1 |
Sider (fra-til) | 1-7 |
Antal sider | 7 |
ISSN | 2053-230X |
DOI | |
Status | Udgivet - 2023 |
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Publisher Copyright:
open access.
ID: 335422968