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CSA entry for 1e6e
Original Entry
Title:
Oxidoreductase
Compound:
Adrenodoxin
Mutant:
No
UniProt/Swiss-Prot:
P00257-ADX1_BOVIN
P08165-ADRO_BOVIN
EC Class:
1.18.1.2
Other CSA Entries:
Overview of all sites for 1e6e
Homologues of 1e6e
Entries for UniProt/Swiss-Prot: P00257
Entries for UniProt/Swiss-Prot: P08165
Entries for EC: 1.18.1.2
Other Databases:
PDB entry: 1e6e
PDBsum entry: 1e6e
UniProt/Swiss-Prot: P00257
UniProt/Swiss-Prot: P08165
IntEnz entry: 1.18.1.2
Literature Report:
Introduction:
Bovine adrenodoxin (Adx) is a ferredoxin involved in the electron transfer from the flavoenzyme NADPH-adrenodoxin-reductase (AdR) to two P450 cytochromes; this process occurs in the production of steroid hormones.
Mechanism:
1) AdR has a bound FAD cofactor. NADPH docks and transfers its hydride to FAD.

2) An electron from FADH- is transferred, via the main chain atoms of Ile 376 and then Thr 377, to the bound half of an Adx dimer (to its Cys 52, then to the [2Fe-2S] centre). The electron is then transferred to the non-AdR-bound Adx molecule which dissociates.

3) The second electron from FADH. is transferred the remaining Adx by the same route; this is concomitant with proton transfer from FADH. to a water molecule bound, and made more basic, by Asp 159 and His 55.
Sites:

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Found by:
Literature reference 

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
HISA 55 87Sidechain
ElectrostaticWater
His 55 binds water and makes it more basic.
Evidence from paper Evidence concerns Evidence type
PubMed ID 10998235 Current protein Residue is positioned appropriately (ligand position known)

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
ASPA 159 191Sidechain
ElectrostaticWater
Asp 159 binds water and makes it more basic.
Evidence from paper Evidence concerns Evidence type
PubMed ID 10998235 Current protein Residue is positioned appropriately (ligand position known)

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
ILEA 376 408Backbone amide, Backbone carbonyl
Electron donor/acceptorResidue
The main chain of Ile 276 is part of an electron transfer chain from FADH- and FADH. to adrenodoxin.
Evidence from paper Evidence concerns Evidence type
PubMed ID 11053423 Current protein Computer modelling
PubMed ID 11053423 Current protein Residue is positioned appropriately (ligand position known)

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
THRA 377 409Backbone amide, Backbone carbonyl
Electron donor/acceptorSubstrate
The main chain of Thr 377 is part of an electron transfer chain from FADH- and FADH. to adrenodoxin.
Evidence from paper Evidence concerns Evidence type
PubMed ID 11053423 Current protein Residue is positioned appropriately (ligand position known)
PubMed ID 11053423 Current protein Computer modelling

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
FADA 461 0
Electron donor/acceptorResidue
Is reduced (by hydride transfer) by NADPH; the two electrons are then passed, one at a time, via main chain residues to the adrenodoxin substrate.
Evidence from paper Evidence concerns Evidence type
PubMed ID 12069587 Current protein Ligand is essential for catalysis
PubMed ID 11053423 Current protein Computer modelling
PubMed ID 12069587 Current protein Residue is positioned appropriately (ligand position known)
Notes:

References:
1
Adrenodoxin reductase-adrenodoxin complex structure suggests electron transfer path in steroid biosynthesis.
J. J. Müller and A. Lapko and G. Bourenkov and K. Ruckpaul and U. Heinemann
J Biol Chem 276, (4) 2786-9, (2001).
11053423
2
A new electron transport mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of adrenodoxin.
D. Beilke and R. Weiss and F. Löhr and P. Pristovsek and F. Hannemann and R. Bernhardt and H. Rüterjans
Biochemistry 41, (25) 7969-78, (2002).
12069587
3
Crystal structures of adrenodoxin reductase in complex with NADP+ and NADPH suggesting a mechanism for the electron transfer of an enzyme family.
G. A. Ziegler and G. E. Schulz
Biochemistry 39, (36) 10986-95, (2000).
10998235
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