1cjc: Difference between revisions
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|PDB= 1cjc |SIZE=350|CAPTION= <scene name='initialview01'>1cjc</scene>, resolution 1.7Å | |PDB= 1cjc |SIZE=350|CAPTION= <scene name='initialview01'>1cjc</scene>, resolution 1.7Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene> | |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] | |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> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cjc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cjc OCA], [http://www.ebi.ac.uk/pdbsum/1cjc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cjc RCSB]</span> | |||
}} | }} | ||
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[[Category: Vonrhein, C.]] | [[Category: Vonrhein, C.]] | ||
[[Category: Ziegler, G A.]] | [[Category: Ziegler, G A.]] | ||
[[Category: electron transferase]] | [[Category: electron transferase]] | ||
[[Category: flavoenzyme]] | [[Category: flavoenzyme]] | ||
[[Category: mad analysis]] | [[Category: mad analysis]] | ||
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Revision as of 19:22, 30 March 2008
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, resolution 1.7Å | |||||||
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Ligands: | |||||||
Activity: | Ferredoxin--NADP(+) reductase, with EC number 1.18.1.2 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
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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