Chemical shift assignments for the apo-form of the catalytic domain, the linker region, and the carbohydrate-binding domain of the cellulose-active lytic polysaccharide monooxygenase ScLPMO10C

Biomol NMR Assign. 2017 Oct;11(2):257-264. doi: 10.1007/s12104-017-9759-2. Epub 2017 Aug 18.

Abstract

The apo-form of the 21.4 kDa catalytic domain and the 10.7 kDa carbohydrate binding domain of the AA10 family lytic polysaccharide monooxygenase ScLPMO10C from Streptomyces coelicolor have been isotopically labeled and recombinantly expressed in Escherichia coli. In this paper, we report the 1H, 13C, and 15N chemical shift assignments of each individual domain as well as an ensemble of the assignment for the full-length protein, including its approximately 30-amino acid long linker.

Keywords: AA10; CBM2; Cellulose; LPMO; Linker; Lytic polysaccharide monooxygenase.

MeSH terms

  • Apoenzymes / chemistry*
  • Apoenzymes / metabolism*
  • Catalytic Domain*
  • Cellulose / metabolism*
  • Mixed Function Oxygenases / chemistry*
  • Mixed Function Oxygenases / metabolism*
  • Nuclear Magnetic Resonance, Biomolecular*
  • Substrate Specificity

Substances

  • Apoenzymes
  • Cellulose
  • Mixed Function Oxygenases