1cjc: Difference between revisions

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-[[Image:1cjc.gif|left|200px]]<br /><applet load="1cjc" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1cjc, resolution 1.7&Aring;" />
-'''STRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMS'''<br />
-==Overview==
+==STRUCTURE OF ADRENODOXIN REDUCTASE OF MITOCHONDRIAL P450 SYSTEMS==
-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.
+<StructureSection load='1cjc' size='340' side='right'caption='[[1cjc]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+== Structural highlights ==
+<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>
+</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>
+<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>
+<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>
+</table>
+== Function ==
+[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.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cj/1cjc_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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==
+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>
-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].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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]
+</div>
+<div class="pdbe-citations 1cjc" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Adrenodoxin reductase 3D structures|Adrenodoxin reductase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Bos taurus]]
-[[Category: Ferredoxin--NADP(+) reductase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Schulz GE]]
-[[Category: Schulz, G.E.]]
+[[Category: Vonrhein C]]
-[[Category: Vonrhein, C.]]
+[[Category: Ziegler GA]]
-[[Category: Ziegler, G.A.]]
-[[Category: FAD]]
-[[Category: electron transferase]]
-[[Category: flavoenzyme]]
-[[Category: mad analysis]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:30:41 2007''