The structure of NADH peroxidase from Streptococcus faecalis at 3.3 A resolution.
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.
Stehle
T
T
Institut für Organische Chemie und Biochemie, Freiburg, FRG.
Ahmed
S A
SA
Claiborne
A
A
Schulz
G E
GE
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
D005182:Flavin-Adenine Dinucleotide; D010544:Peroxidases; C021845:NAD+ peroxidase; D003545:Cysteine