title: The structure of NADH peroxidase from Streptococcus faecalis at 3.3 A resolution.
abstract: NADH peroxidase (EC 1.11.1.1) previously isolated from Streptococcus faecalis 10C1 has been crystallized. The crystal structure has been solved by multiple isomorphous replacement and solvent-flattening at 3.3 A (1 A = 0.1 nm) resolution. The enzyme forms a tetramer consisting of 4 crystallographically related subunits. The monomer chain fold is in general similar to those of glutathione reductase and lipoamide dehydrogenase. FAD binds in the same region and in a similar conformation as in glutathione reductase. The unusual cysteine-sulfenic acid participating in catalysis is located at the isoalloxazine of FAD.
authors.affiliation: Institut für Organische Chemie und Biochemie, Freiburg, FRG.
authors.forename: T
authors.initials: T
authors.lastname: Stehle
authors.forename: S A
authors.initials: SA
authors.lastname: Ahmed
authors.forename: A
authors.initials: A
authors.lastname: Claiborne
authors.forename: G E
authors.initials: GE
authors.lastname: Schulz
mesh_terms: D003460:Crystallization; D003545:Cysteine; D013293:Enterococcus faecalis / Q000201:enzymology*; D005182:Flavin-Adenine Dinucleotide; D008958:Models, Molecular; D010544:Peroxidases / Q000032:analysis* / Q000302:isolation & purification; D011487:Protein Conformation; D014961:X-Ray Diffraction
chemical_list: D005182:Flavin-Adenine Dinucleotide; D010544:Peroxidases; C021845:NAD+ peroxidase; D003545:Cysteine