1cjc: Difference between revisions

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[[Image:1cjc.gif|left|200px]]<br /><applet load="1cjc" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1cjc.gif|left|200px]]
caption="1cjc, resolution 1.7&Aring;" />
 
'''STRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMS'''<br />
{{Structure
|PDB= 1cjc |SIZE=350|CAPTION= <scene name='initialview01'>1cjc</scene>, resolution 1.7&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene>
|ACTIVITY= [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]
|GENE=
}}
 
'''STRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMS'''
 


==Overview==
==Overview==
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==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 <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].  
1CJC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CJC OCA].  


==Reference==
==Reference==
The structure of adrenodoxin reductase of mitochondrial P450 systems: electron transfer for steroid biosynthesis., Ziegler GA, Vonrhein C, Hanukoglu I, Schulz GE, J Mol Biol. 1999 Jun 18;289(4):981-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10369776 10369776]
The structure of adrenodoxin reductase of mitochondrial P450 systems: electron transfer for steroid biosynthesis., Ziegler GA, Vonrhein C, Hanukoglu I, Schulz GE, J Mol Biol. 1999 Jun 18;289(4):981-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10369776 10369776]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Ferredoxin--NADP(+) reductase]]
[[Category: Ferredoxin--NADP(+) reductase]]
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[[Category: mad analysis]]
[[Category: mad analysis]]


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Revision as of 11:25, 20 March 2008

File:1cjc.gif


PDB ID 1cjc

Drag the structure with the mouse to rotate
, resolution 1.7Å
Ligands:
Activity: Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMS


OverviewOverview

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 StructureAbout this Structure

1CJC is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

The structure of adrenodoxin reductase of mitochondrial P450 systems: electron transfer for steroid biosynthesis., Ziegler GA, Vonrhein C, Hanukoglu I, Schulz GE, J Mol Biol. 1999 Jun 18;289(4):981-90. PMID:10369776

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