1cjc: Difference between revisions

New page: left|200px<br /><applet load="1cjc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cjc, resolution 1.7Å" /> '''STRUCTURE OF ADRENODO...
 
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caption="1cjc, resolution 1.7&Aring;" />
'''STRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMS'''<br />
'''STRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMS'''<br />


==Overview==
==Overview==
Adrenodoxin reductase is a monomeric 51 kDa flavoenzyme that is involved, in the biosynthesis of all steroid hormones. The structure of the native, bovine enzyme was determined at 2.8 A resolution, and the structure of the, respective recombinant enzyme at 1.7 A resolution. Adrenodoxin reductase, receives a two-electron package from NADPH and converts it to two single, electrons that are transferred via adrenodoxin to all mitochondrial, cytochromes P 450. The structure suggests how the observed flavin, semiquinone is stabilized. A striking feature is the asymmetric charge, distribution, which most likely controls the approach of the electron, carrier adrenodoxin. A model for the interaction is proposed. Adrenodoxin, reductase shows clear sequence homology to half a dozen proteins, identified in genome analysis projects, but neither sequence nor, structural homology to established, functionally related electron, transferases. Yet, the structure revealed a relationship to the disulfide, oxidoreductases, permitting the assignment of the NADP-binding site.
Adrenodoxin reductase is a monomeric 51 kDa flavoenzyme that is involved in the biosynthesis of all steroid hormones. The structure of the native bovine enzyme was determined at 2.8 A resolution, and the structure of the respective recombinant enzyme at 1.7 A resolution. Adrenodoxin reductase receives a two-electron package from NADPH and converts it to two single electrons that are transferred via adrenodoxin to all mitochondrial cytochromes P 450. The structure suggests how the observed flavin semiquinone is stabilized. A striking feature is the asymmetric charge distribution, which most likely controls the approach of the electron carrier adrenodoxin. A model for the interaction is proposed. Adrenodoxin reductase shows clear sequence homology to half a dozen proteins identified in genome analysis projects, but neither sequence nor structural homology to established, functionally related electron transferases. Yet, the structure revealed a relationship to the disulfide oxidoreductases, permitting the assignment of the NADP-binding site.


==About this Structure==
==About this Structure==
1CJC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with FAD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ferredoxin--NADP(+)_reductase Ferredoxin--NADP(+) reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.1.2 1.18.1.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CJC OCA].  
1CJC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ferredoxin--NADP(+)_reductase Ferredoxin--NADP(+) reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.1.2 1.18.1.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CJC OCA].  


==Reference==
==Reference==
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[[Category: Ferredoxin--NADP(+) reductase]]
[[Category: Ferredoxin--NADP(+) reductase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Schulz, G.E.]]
[[Category: Schulz, G E.]]
[[Category: Vonrhein, C.]]
[[Category: Vonrhein, C.]]
[[Category: Ziegler, G.A.]]
[[Category: Ziegler, G A.]]
[[Category: FAD]]
[[Category: FAD]]
[[Category: electron transferase]]
[[Category: electron transferase]]
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[[Category: mad analysis]]
[[Category: mad analysis]]


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