The effect of linker conformation on performance and stability of a two-domain lytic polysaccharide monooxygenase.

ABSTRACT: A considerable number of lytic polysaccharide monooxygenases (LPMOs) and other carbohydrate-active enzymes are modular, with catalytic domains being tethered to additional domains, such as carbohydrate-binding modules, by flexible linkers. While such linkers may affect the structure, function, and stability of the enzyme, their roles remain largely enigmatic, as do the reasons for natural variation in length and sequence. Here, we have explored linker functionality using the two-domain cellulose-active ScLPMO10C from Streptomyces coelicolor as a model system. In addition to investigating the WT enzyme, we engineered three linker variants to address the impact of both length and sequence and characterized these using small-angle X-ray scattering, NMR, molecular dynamics simulations, and fun

SUBMITTER: Forsberg Z 

PROVIDER: S-EPMC10598543 | biostudies-literature | 2023 Nov

REPOSITORIES: biostudies-literature