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

FEBS Letters

Stehle, T.¹  Schulz, G.E.¹  Claiborne, A.²  Ahmed, S.A.² 

[1] Institut für Organische Chemie und Biochemie, Albertstr. 21, D-7800 Freiburg i. Br., FRG;Wake Forest University Medical Center, Department of Biochemistry, 300 South Hawthorne Road, Winston-Salem, NC 27103, USA

关键词: NADH peroxidase;    Flavoenzyme;    X-ray structure;    Cysteine-sulfenic acid;    Streptococcus faecalis;    GR;    glutathione reductase;    LPDH;    lipoamide dehydrogenase;    m.i.r.;    multiple isomorphous replacement;    NPX;    NADH peroxidase;   

DOI  :  10.1016/0014-5793(90)80921-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Å (1 Å = 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.

【 授权许可】

Unknown