3B3R: Crystal structure of Streptomyces cholesterol oxidase H447Q/E361Q mutant bound to glycerol (0.98A)

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 structure, indicating that some tuning of the FAD redox potential is caused by the formation of the Michaelis complex during regular catalysis. This structural study suggests a possible mechanism of substrate-assisted flavin activation, improves our understanding of the interplay between the enzyme, its flavin cofactor and its substrate, and is of use to the future design of effective cholesterol oxidase inhibitors.
PDB ID: 3B3RDownload
MMDB ID: 163290
PDB Deposition Date: 2007/10/22
Updated in MMDB: 2018/06
Experimental Method:
x-ray diffraction
Resolution: 0.98  Å
Source Organism:
Similar Structures:
Biological Unit for 3B3R: monomeric; determined by author and by software (PISA)
Molecular Components in 3B3R
Label Count Molecule
Protein (1 molecule)
Cholesterol Oxidase
Molecule annotation
Chemicals (6 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB