Structural perturbations of substrate binding and oxidation state changes in a lytic polysaccharide monooxygenase.

ABSTRACT: LPMOs are enzymes which catalyse the oxidation of a C-H bond within polysaccharides, leading to their oxidative cleavage. To achieve this, LPMOs employ highly reactive oxidising intermediates, the generation of which is likely coupled to substrate binding to the enzyme. The nature of this coupling is unknown. Here we report a statistical comparison for four three-dimensional structures of an AA9 LPMO crystallised in the same space group but in different oxidation and substrate-binding states, to determine which significant structural perturbations occur at the enzyme upon either oxidation state change or the binding of substrate. In a novel step, we determine the global random error associated with the positional coordinates of atoms using the method of moments to ascertain the statistical

SUBMITTER: Walton PH 

PROVIDER: S-EPMC9653361 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature