FEBS Letters | |
The structure of NADH peroxidase from Streptococcus faecalis at 3.3 Å resolution | |
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
【 预 览 】
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RO201912020293579ZK.pdf | 330KB | download |