The structure of NADH peroxidase from Streptococcus faecalis at 3.3 A resolution

FEBS Lett. 1990 Jul 16;267(2):186-8. doi: 10.1016/0014-5793(90)80921-5.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Crystallization
  • Cysteine
  • Enterococcus faecalis / enzymology*
  • Flavin-Adenine Dinucleotide
  • Models, Molecular
  • Peroxidases / analysis*
  • Peroxidases / isolation & purification
  • Protein Conformation
  • X-Ray Diffraction

Substances

  • Flavin-Adenine Dinucleotide
  • Peroxidases
  • NAD+ peroxidase
  • Cysteine