1ndh
From Proteopedia
(New page: 200px<br /><applet load="1ndh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ndh, resolution 2.1Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1ndh.jpg|left|200px]]<br /><applet load="1ndh" size=" | + | [[Image:1ndh.jpg|left|200px]]<br /><applet load="1ndh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ndh, resolution 2.1Å" /> | caption="1ndh, resolution 2.1Å" /> | ||
'''CRYSTAL STRUCTURE OF NADH-CYTOCHROME B5 REDUCTASE FROM PIG LIVER AT 2.4 ANGSTROMS RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE OF NADH-CYTOCHROME B5 REDUCTASE FROM PIG LIVER AT 2.4 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of NADH-cytochrome b5 reductase from pig | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1NDH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with FAD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cytochrome-b5_reductase Cytochrome-b5 reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.2.2 1.6.2.2] Full crystallographic information is available from [http:// | + | 1NDH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cytochrome-b5_reductase Cytochrome-b5 reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.2.2 1.6.2.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NDH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: electron transport (flavo protein)]] | [[Category: electron transport (flavo protein)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:05:00 2008'' |
Revision as of 12:05, 21 February 2008
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CRYSTAL STRUCTURE OF NADH-CYTOCHROME B5 REDUCTASE FROM PIG LIVER AT 2.4 ANGSTROMS RESOLUTION
Overview
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.
About this Structure
1NDH is a Single protein structure of sequence from Sus scrofa with as ligand. Active as Cytochrome-b5 reductase, with EC number 1.6.2.2 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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