open access publication

Article, 2023

Joint X‐ray/neutron structure of Lentinus similis AA9_A at room temperature

In: Acta Crystallographica Section F: Structural Biology Communications, ISSN 1744-3091, 2053-230X, Volume 79, 1, Pages 1-7, 10.1107/s2053230x22011335

Contributors (3)

Tandrup, Tobias (0000-0002-3448-7019) [1] Leggio, Leila Lo (0000-0002-5135-0882) [1] Meilleur, Flora (0000-0001-9313-8989) (Corresponding author) [2] [3]

Affiliations

  1. [1] University of Copenhagen
  2. [NORA names: KU University of Copenhagen; University; Denmark; Europe, EU; Nordic; OECD]
  3. [2] North Carolina State University
  4. [NORA names: United States; America, North; OECD]
  5. [3] Oak Ridge National Laboratory
  6. [NORA names: United States; America, North; OECD]

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.

Keywords

AA9, Lentinus similis, X-ray, X-ray crystallography, activity, biology, biotechnology, carbon cycling, characterization, complexes, copper metalloenzymes, crystallographic structure, crystallographic studies, crystallography, cycling, data, detailed structural characterization, determination, experimental determination, family AA9, high resolution, interaction, lytic polysaccharide monooxygenases, metalloenzymes, model system, monooxygenases, neutron crystallographic study, neutron data, neutron structure, pathogen biology, polysaccharide monooxygenases, polysaccharides, protonation state, residues, resolution, results, room temperature, saccharide substrates, second-shell residues, similis, state, structural characterization, structure, study, substrate, system, temperature, variety, variety of substrates, way

Funders

  • Danish Agency for Science and Higher Education
  • National Institute of Food and Agriculture
  • Novo Nordisk Foundation
  • Oak Ridge National Laboratory
  • Office of Basic Energy Sciences