1NDH

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

Summary for 1NDH

• Entry DOI: 10.2210/pdb1ndh/pdb
• Descriptor: CYTOCHROME B5 REDUCTASE, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: electron transport (flavo protein)
• Biological source: Sus scrofa (pig)
• Total number of polymer chains: 1
• Total formula weight: 31659.22

Authors

Nishida, H.,Miki, K. (deposition date: 1994-10-31, release date: 1995-02-14, Last modification date: 2024-02-14)

Primary citation

Nishida, H.,Inaka, K.,Yamanaka, M.,Kaida, S.,Kobayashi, K.,Miki, K.
Crystal structure of NADH-cytochrome b5 reductase from pig liver at 2.4 A resolution.
Biochemistry, 34:2763-2767, 1995

PubMed Abstract: 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.

PubMed: 7893687
DOI: 10.1021/bi00009a004

Experimental method

X-RAY DIFFRACTION (2.1 Å)