Structural highlights
Publication Abstract from PubMed
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 (1)H, (13)C, and (15)N 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.
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.,Courtade G, Forsberg Z, Vaaje-Kolstad G, Eijsink VGH, Aachmann FL Biomol NMR Assign. 2017 Oct;11(2):257-264. doi: 10.1007/s12104-017-9759-2. Epub, 2017 Aug 18. PMID:28822070[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Courtade G, Forsberg Z, Vaaje-Kolstad G, Eijsink VGH, Aachmann FL. 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. PMID:28822070 doi:http://dx.doi.org/10.1007/s12104-017-9759-2
