1e1l: Difference between revisions

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[[Image:1e1l.jpg|left|200px]]
[[Image:1e1l.jpg|left|200px]]


{{Structure
<!--
|PDB= 1e1l |SIZE=350|CAPTION= <scene name='initialview01'>1e1l</scene>, resolution 2.3&Aring;
The line below this paragraph, containing "STRUCTURE_1e1l", creates the "Structure Box" on the page.
|SITE= <scene name='pdbsite=AC1:Nap+Binding+Site+For+Chain+A'>AC1</scene> and <scene name='pdbsite=AC2:Fad+Binding+Site+For+Chain+A'>AC2</scene>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[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] </span>
or leave the SCENE parameter empty for the default display.
|GENE=  
-->
|DOMAIN=
{{STRUCTURE_1e1l| PDB=1e1l  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e1l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e1l OCA], [http://www.ebi.ac.uk/pdbsum/1e1l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e1l RCSB]</span>
}}


'''STRUCTURE OF ADRENODOXIN REDUCTASE IN COMPLEX WITH NADP OBTAINED BY COCRYSTALLISATION'''
'''STRUCTURE OF ADRENODOXIN REDUCTASE IN COMPLEX WITH NADP OBTAINED BY COCRYSTALLISATION'''
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Crystal structures of adrenodoxin reductase in complex with NADP+ and NADPH suggesting a mechanism for the electron transfer of an enzyme family., Ziegler GA, Schulz GE, Biochemistry. 2000 Sep 12;39(36):10986-95. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10998235 10998235]
Crystal structures of adrenodoxin reductase in complex with NADP+ and NADPH suggesting a mechanism for the electron transfer of an enzyme family., Ziegler GA, Schulz GE, Biochemistry. 2000 Sep 12;39(36):10986-95. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10998235 10998235]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Ferredoxin--NADP(+) reductase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Schulz, G E.]]
[[Category: Schulz, G E.]]
[[Category: Ziegler, G A.]]
[[Category: Ziegler, G A.]]
[[Category: electron transferase]]
[[Category: Electron transferase]]
[[Category: flavoenzyme]]
[[Category: Flavoenzyme]]
[[Category: nadp]]
[[Category: Nadp]]
[[Category: oxidoreductase]]
[[Category: Oxidoreductase]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:53:09 2008''

Revision as of 14:32, 2 May 2008

File:1e1l.jpg

Template:STRUCTURE 1e1l

STRUCTURE OF ADRENODOXIN REDUCTASE IN COMPLEX WITH NADP OBTAINED BY COCRYSTALLISATION


OverviewOverview

Adrenodoxin reductase is a flavoenzyme that shuffles electrons for the biosynthesis of steroids. Its chain topology belongs to the glutathione reductase family of disulfide oxidoreductases, all of which bind FAD at equivalent positions. The three reported structures of adrenodoxin reductase were ligated with reduced and oxidized NADP and have now confirmed this equivalence also for the NADP-binding site. Remarkably, the conformations and relative positions of the prosthetic group FAD and the cofactor NADP have been conserved during protein evolution despite very substantial changes in the polypeptide. The ligated enzymes showed small changes in the domain positions. When compared with the structure of the NADP-free enzyme, these positions correspond to several states of the domain motion during NADP binding. On the basis of the observed structures, we suggest an enzymatic mechanism for the subdivision of the received two-electron package into the two single electrons transferred to the carrier protein adrenodoxin. The data banks contain 10 sequences that are closely related to bovine adrenodoxin reductase. Most of them code for gene products with unknown functions. Within this family, the crucial residues of adrenodoxin reductase are strictly conserved. Moreover, the putative docking site of the carrier is rather well conserved. Five of the family members were assigned names related to ferredoxin:NADP(+) reductase, presumably because adrenodoxin reductase was considered a member of this functionally similar family. Since this is not the case, the data bank entries should be corrected.

About this StructureAbout this Structure

1E1L is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of adrenodoxin reductase in complex with NADP+ and NADPH suggesting a mechanism for the electron transfer of an enzyme family., Ziegler GA, Schulz GE, Biochemistry. 2000 Sep 12;39(36):10986-95. PMID:10998235 Page seeded by OCA on Fri May 2 14:32:43 2008

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