Structure of NADH peroxidase from Streptococcus faecalis 10C1 refined at 2.16 A resolution.
The crystal structure of NADH peroxidase (EC 1.11.1.1) from Streptococcus faecalis 10C1 (Enterococcus faecalis) has been refined to a resolution of 2.16 A using the simulated annealing method. The final crystallographic R-factor is 17.7% for all data in the resolution range 7 to 2.16 A. The standard deviations are 0.015 A in bond lengths and 3.0 degrees in bond angles for the final model, which includes all 447 amino acid residues, one FAD and 369 water molecules. The enzyme is a symmetrical tetramer with point group D2; the symmetry is crystallographic. The redox center of the enzyme consists of FAD and a cysteine (Cys42), which forms a sulfenic acid (Cys-SOH) in its oxidized state. A histidine (His10) close to Cys42 is likely to act as an active-site base. In the analyzed crystal, the enzyme was in a non-native oxidation state with Cys42 oxidized to a sulfonic acid Cys-SO3H. The chain fold of NADH peroxidase is similar to those of disulfide oxidoreductases. A comparison with glutathione reductase, a representative of this enzyme family, is given.
Stehle
T
T
Institut für Organische Chemie und Biochemie der Universität, Freiburg, Germany.
Ahmed
S A
SA
Claiborne
A
A
Schulz
G E
GE
D000595:Amino Acid Sequence; D001665:Binding Sites / Q000502:physiology; D003460:Crystallization; D003544:Cysteic Acid / Q000737:chemistry; D013293:Enterococcus faecalis / Q000201:enzymology*; D005980:Glutathione Reductase / Q000737:chemistry; D046911:Macromolecular Substances; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000737:chemistry* / Q000302:isolation & purification; D011487:Protein Conformation; D014961:X-Ray Diffraction
D046911:Macromolecular Substances; D003544:Cysteic Acid; D010544:Peroxidases; C021845:NAD+ peroxidase; D005980:Glutathione Reductase