8E1W
Neutron crystal structure of Panus similis AA9A at room temperature
Summary for 8E1W
| Entry DOI | 10.2210/pdb8e1w/pdb |
| Descriptor | Endo-beta-1,4-glucanase D, COPPER (II) ION, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | beta sandwiches, glycosylated, oxidoreductase |
| Biological source | Panus similis |
| Total number of polymer chains | 1 |
| Total formula weight | 25593.06 |
| Authors | Meilleur, F.,Tandrup, T.,Lo Leggio, L. (deposition date: 2022-08-11, release date: 2023-01-11, Last modification date: 2024-04-03) |
| Primary citation | Tandrup, T.,Lo Leggio, L.,Meilleur, F. Joint X-ray/neutron structure of Lentinus similis AA9_A at room temperature. Acta Crystallogr.,Sect.F, 79:1-7, 2023 Cited by PubMed 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. PubMed: 36598350DOI: 10.1107/S2053230X22011335 PDB entries with the same primary citation |
| Experimental method | NEUTRON DIFFRACTION (2.8 Å) X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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