1NPX

STRUCTURE OF NADH PEROXIDASE FROM STREPTOCOCCUS FAECALIS 10C1 REFINED AT 2.16 ANGSTROMS RESOLUTION

Summary for 1NPX

• Entry DOI: 10.2210/pdb1npx/pdb
• Descriptor: NADH PEROXIDASE, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: oxidoreductase(h2o2(a))
• Biological source: Enterococcus faecalis
• Total number of polymer chains: 1
• Total formula weight: 50436.78

Authors

Stehle, T.,Ahmed, S.A.,Claiborne, A.,Schulz, G.E. (deposition date: 1991-08-02, release date: 1994-01-31, Last modification date: 2024-06-05)

Primary citation

Stehle, T.,Ahmed, S.A.,Claiborne, A.,Schulz, G.E.
Structure of NADH peroxidase from Streptococcus faecalis 10C1 refined at 2.16 A resolution.
J.Mol.Biol., 221:1325-1344, 1991

PubMed Abstract: 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.

PubMed: 1942054

Experimental method

X-RAY DIFFRACTION (2.16 Å)