1cjc

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(New page: 200px<br /><applet load="1cjc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cjc, resolution 1.7&Aring;" /> '''STRUCTURE OF ADRENODO...)
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[[Image:1cjc.gif|left|200px]]<br /><applet load="1cjc" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cjc, resolution 1.7&Aring;" />
 
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'''STRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMS'''<br />
 
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==Overview==
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==STRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMS==
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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.
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<StructureSection load='1cjc' size='340' side='right'caption='[[1cjc]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cjc]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CJC FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cjc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cjc OCA], [https://pdbe.org/1cjc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cjc RCSB], [https://www.ebi.ac.uk/pdbsum/1cjc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cjc ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ADRO_BOVIN ADRO_BOVIN] Serves as the first electron transfer protein in all the mitochondrial P450 systems. Including cholesterol side chain cleavage in all steroidogenic tissues, steroid 11-beta hydroxylation in the adrenal cortex, 25-OH-vitamin D3-24 hydroxylation in the kidney, and sterol C-27 hydroxylation in the liver.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cj/1cjc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cjc ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:10369776</ref>
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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].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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]
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</div>
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[[Category: Bos taurus]]
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<div class="pdbe-citations 1cjc" style="background-color:#fffaf0;"></div>
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[[Category: Ferredoxin--NADP(+) reductase]]
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[[Category: Single protein]]
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[[Category: Schulz, G.E.]]
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[[Category: Vonrhein, C.]]
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[[Category: Ziegler, G.A.]]
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[[Category: FAD]]
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[[Category: electron transferase]]
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[[Category: flavoenzyme]]
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[[Category: mad analysis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:30:41 2007''
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==See Also==
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*[[Adrenodoxin reductase 3D structures|Adrenodoxin reductase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bos taurus]]
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[[Category: Large Structures]]
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[[Category: Schulz GE]]
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[[Category: Vonrhein C]]
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[[Category: Ziegler GA]]

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STRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMS

PDB ID 1cjc

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