Joint X‐ray/neutron structure of Lentinus similis AA9_A at room temperature. Issue 1 (8th December 2022)

• Record Type: Journal Article
• Authors: Tandrup, Tobias; Lo Leggio, Leila; Meilleur, Flora
• Is Part Of: Acta crystallographica. Volume 79:Issue 1(2023)
• Page Start: 1
• Page End: 7
• Publication Date: 2022-12-08
• Subjects: lytic polysaccharide monooxygenases -- Lentinus similis AA9_A -- copper metalloenzymes -- protonation states -- neutron crystallography; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X22011335
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : The room‐temperature structure of Lentinus similis AA9_A was refined jointly against X‐ray and neutron crystallographic data extending to 2.1 and 2.8 Å resolution, respectively. 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 ( Ls AA9_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 Ls AA9_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 Ls AA9_A, paving the way for future neutron crystallographic studies of LPMO–carbohydrate complexes.