CRYSTAL-STRUCTURE OF NADH-CYTOCHROME-B5 REDUCTASE FROM PIG-LIVER AT 2.4-ANGSTROM RESOLUTION

被引：83

作者：

NISHIDA, H

INAKA, K

YAMANAKA, M

KAIDA, S

KOBAYASHI, K

MIKI, K

机构：

[1] TOKYO INST TECHNOL, RESOURCES UTILIZAT RES LAB, MIDORI KU, YOKOHAMA, KANAGAWA 227, JAPAN

[2] OSAKA UNIV, FAC ENGN, DEPT APPL CHEM, SUITA, OSAKA 565, JAPAN

[3] OSAKA UNIV, INST SCI & IND RES, IBARAKI, OSAKA 567, JAPAN

来源：

BIOCHEMISTRY | 1995年 / 34卷 / 09期

关键词：

D O I：

10.1021/bi00009a004

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The three-dimensional structure of NADH-cytochrome bs reductase from pig liver microsomes has been determined at 2.4 Angstrom resolution by X-ray crystallography. The molecular structure reveals two domains, the FAD binding domain and the NADH domain. A large cleft Lies between these two domains and contains the binding site for the FAD prosthetic group. The backbone structure of the FAD binding domain has a great similarity to that of ferredoxin-NADP(+) reductase [Karplus, P. A., Daniels, M. J., & Herriott, J. R. (1991) Science 251, 60-65], in spite of the relatively low sequence homology (about 15%) between the two enzymes. On the other hand, the structure of the NADH domain has several structural differences from that of the NADP(+) domain of ferredoxin-NADP(+) reductase. The size of the cleft between the two domains is larger in NADH-cytochrome b(5) reductase than in ferredoxin-NADP(+) reductase, which may be responsible for the observed difference in the nucleotide accessibility in the two enzymes.

引用

页码：2763 / 2767

页数：5