Revealing Hidden Conformational Space of LOV Protein VIVID Through Rigid Residue Scan Simulations.

ABSTRACT: VIVID(VVD) protein is a Light-Oxygen-Voltage(LOV) domain in circadian clock system. Upon blue light activation, a covalent bond is formed between VVD residue Cys108 and its cofactor flavin adenine dinucleotide(FAD), and prompts VVD switching from Dark state to Light state with significant conformational deviation. However, the mechanism of this local environment initiated global protein conformational change remains elusive. We employed a recently developed computational approach, rigid residue scan(RRS), to systematically probe the impact of the internal degrees of freedom in each amino acid residue of VVD on its overall dynamics by applying rigid body constraint on each residue in molecular dynamics simulations. Key residues were identified with distinctive impacts on Dark and Light stat

SUBMITTER: Zhou H 

PROVIDER: S-EPMC5397860 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature