Structure of a Thermobifida fusca lytic polysaccharide monooxygenase and mutagenesis of key residues.

ABSTRACT:

Background

Auxiliary activity (AA) enzymes are produced by numerous bacterial and fungal species to assist in the degradation of biomass. These enzymes are abundant but have yet to be fully characterized. Here, we report the X-ray structure of Thermobifida fusca AA10A (TfAA10A), investigate mutational characterization of key surface residues near its active site, and explore the importance of the various domains of Thermobifida fusca AA10B (TfAA10B). The structure of TfAA10A is similar to other bacterial LPMOs (lytic polysaccharide monooxygenases), including signs of photo-reduction and a distorted active site, with mixed features showing both type I and II copper coordination. The point mutation experiments of TfAA10A show that Trp82 and Asn83 are needed for binding,

SUBMITTER: Kruer-Zerhusen N 

PROVIDER: S-EPMC5708082 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature