1cjc: Difference between revisions

Revision as of 13:06, 21 February 2008

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 with as ligand. Active as Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2 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

Page seeded by OCA on Thu Feb 21 12:06:40 2008

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OCA

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-[[Image:1cjc.gif|left|200px]]<br /><applet load="1cjc" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1cjc.gif|left|200px]]<br /><applet load="1cjc" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1cjc, resolution 1.7&Aring;" />
 '''STRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMS'''<br />
 ==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==
-CJC 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].
+CJC 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==
@@ Line 14: / Line 14: @@
 [[Category: Ferredoxin--NADP(+) reductase]]
 [[Category: Single protein]]
-[[Category: Schulz, G.E.]]
+[[Category: Schulz, G E.]]
 [[Category: Vonrhein, C.]]
-[[Category: Ziegler, G.A.]]
+[[Category: Ziegler, G A.]]
 [[Category: FAD]]
 [[Category: electron transferase]]
@@ Line 22: / Line 22: @@
 [[Category: mad analysis]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:30:41 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:06:40 2008''