1H, 13C, 15N resonance assignment of the apo form of the small, chitin-active lytic polysaccharide monooxygenase JdLPMO10A from Jonesia denitrificans

Abstract

The lytic polysaccharide monooxygenase <i>Jd</i>LPMO10A is the N-terminal domain of the multimodular protein Jd1381. The isolated <i>Jd</i>LPMO10A domain is one of the smallest chitin-active lytic polysaccharide monooxygenases known to date with a size of only 15.5 kDa. <i>Jd</i>LPMO10A is a copper-dependent oxidative enzyme that depolymerizes chitin by hydroxylating the C1 carbon in the glycosidic bond. <i>Jd</i>LPMO10A has been isotopically labeled and recombinantly expressed. Here, we report the ¹H, ¹³C, ¹⁵N resonance assignment of <i>Jd</i>LPMO10A. Secondary structural elements predicted based on the NMR assignment are in excellent agreement with the crystal structure of <i>Jd</i>LPMO10A.