Ontology highlight
ABSTRACT:
SUBMITTER: Lyubimov AY
PROVIDER: S-EPMC2222809 | biostudies-literature | 2007 Dec
REPOSITORIES: biostudies-literature
Protein science : a publication of the Protein Society 20071201 12
Two high-resolution structures of a double mutant of bacterial cholesterol oxidase in the presence or absence of a ligand, glycerol, are presented, showing the trajectory of glycerol as it binds in a Michaelis complex-like position in the active site. A group of three aromatic residues forces the oxidized isoalloxazine moiety to bend along the N5-N10 axis as a response to the binding of glycerol in the active site. Movement of these aromatic residues is only observed in the glycerol-bound struct ...[more]