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Publication Abstract from PubMed

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 A 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.

Joint X-ray/neutron structure of Lentinus similis AA9_A at room temperature.,Tandrup T, Lo Leggio L, Meilleur F Acta Crystallogr F Struct Biol Commun. 2023 Jan 1;79(Pt 1):1-7. doi: , 10.1107/S2053230X22011335. Epub 2023 Jan 1. PMID:36598350^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.