Crystallization and preliminary x-ray crystallographic study of NADH-cytochrome b5 reductase from pig liver microsomes.

Miki, Kunio; Kaida, Satoshi; Kasai, Nobutami; Iyanagi, Takashi; Kobayashi, Kazuo; Hayashi, Koichiro

doi:10.1016/s0021-9258(18)60883-x

Cited by 18 publications

(3 citation statements)

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Section: Methodsmentioning

confidence: 99%

“…The lysosome-solubilized hydrophilic domain of b5R was purified from pig liver microsomes (Iyanagi et al, 1984) and crystallized as described previously (Miki et al, 1987). The crystals belong to the space group R2i2i2i with unit cell dimensions of a -86.9 A, b = 73.1 A, and c = 48.9 A (Miki et al, 1987). The crystal structure was initially solved by multiple isomorphous replacement (MIR) using diffraction data at 2.5 A resolution collected on six different heavyatom derivatives (Table 1).…”

Section: Methodsmentioning

confidence: 99%

“…Both forms of the enzyme were crystallized. The latter form gave crystals suitable for high-resolution X-ray crystallography (Miki et al, 1987). The soluble form of this enzyme from human erythrocytes was also crystallized in a different crystal system (Takano et al, 1987).…”

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confidence: 99%

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Crystal Structure of NADH-Cytochrome b5 Reductase from Pig Liver at 2.4 .ANG. Resolution

Nishida

Inaka²,

Yamanaka³

et al. 1995

Biochemistry

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The three-dimensional structure of NADH-cytochrome b5 reductase from pig liver microsomes has been determined at 2.4 A 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 b5 reductase than in ferredoxin-NADP+ reductase, which may be responsible for the observed difference in the nucleotide accessibility in the two enzymes.

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Section: Methodsmentioning

confidence: 99%