1ndh: Difference between revisions

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{{STRUCTURE_1ndh|  PDB=1ndh  |  SCENE=  }}  
{{STRUCTURE_1ndh|  PDB=1ndh  |  SCENE=  }}  


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




==Overview==
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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., &amp; 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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{{ABSTRACT_PUBMED_7893687}}


==About this Structure==
==About this Structure==
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[[Category: Miki, K.]]
[[Category: Miki, K.]]
[[Category: Nishida, H.]]
[[Category: Nishida, H.]]
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Revision as of 04:44, 28 July 2008

File:1ndh.png

Template:STRUCTURE 1ndh

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

Template:ABSTRACT PUBMED 7893687

About this Structure

1NDH is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

Reference

Crystal structure of NADH-cytochrome b5 reductase from pig liver at 2.4 A resolution., Nishida H, Inaka K, Yamanaka M, Kaida S, Kobayashi K, Miki K, Biochemistry. 1995 Mar 7;34(9):2763-7. PMID:7893687

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