Allosteric Communication in the Multifunctional and Redox NQO1 Protein Studied by Cavity-Making Mutations.

ABSTRACT: Allosterism is a common phenomenon in protein biochemistry that allows rapid regulation of protein stability; dynamics and function. However, the mechanisms by which allosterism occurs (by mutations or post-translational modifications (PTMs)) may be complex, particularly due to long-range propagation of the perturbation across protein structures. In this work, we have investigated allosteric communication in the multifunctional, cancer-related and antioxidant protein NQO1 by mutating several fully buried leucine residues (L7, L10 and L30) to smaller residues (V, A and G) at sites in the N-terminal domain. In almost all cases, mutated residues were not close to the FAD or the active site. Mutations L→G strongly compromised conformational stability and solubility, and L30A and L30V also nota

SUBMITTER: Pacheco-Garcia JL 

PROVIDER: S-EPMC9219786 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature