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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1e6e

E.C. nameferredoxin---NADP+ reductase
SpeciesBos taurus (Bovine)
E.C. Number (IntEnz) 1.18.1.2
CSA Homologues of 1e6e1cjc,1e1k,1e1l,1e1m,1e1n,
CSA Entries With UniProtID P08165
CSA Entries With EC Number 1.18.1.2
PDBe Entry 1e6e
PDBSum Entry 1e6e
MACiE Entry M0142

Literature Report

IntroductionBovine 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.
Mechansim1) 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.

Catalytic Sites for 1e6e

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ThrA377409macie:mainChainAmideThe main chain of Thr 377 is part of an electron transfer chain from FADH- and FADH. to adrenodoxin.
ThrA377409macie:mainChainCarbonylThe main chain of Thr 377 is part of an electron transfer chain from FADH- and FADH. to adrenodoxin.
IleA376408macie:mainChainAmideThe main chain of Ile 276 is part of an electron transfer chain from FADH- and FADH. to adrenodoxin.
IleA376408macie:mainChainCarbonylThe main chain of Ile 276 is part of an electron transfer chain from FADH- and FADH. to adrenodoxin.
HisA5587macie:sideChainHis 55 binds water and makes it more basic.
AspA159191macie:sideChainAsp 159 binds water and makes it more basic.

Annotated By Reference To The Literature - Site 2 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
ThrC377409macie:mainChainAmideThe main chain of Thr 377 is part of an electron transfer chain from FADH- and FADH. to adrenodoxin.
ThrC377409macie:mainChainCarbonylThe main chain of Thr 377 is part of an electron transfer chain from FADH- and FADH. to adrenodoxin.
IleC376408macie:mainChainAmideThe main chain of Ile 276 is part of an electron transfer chain from FADH- and FADH. to adrenodoxin.
IleC376408macie:mainChainCarbonylThe main chain of Ile 276 is part of an electron transfer chain from FADH- and FADH. to adrenodoxin.
HisC5587macie:sideChainHis 55 binds water and makes it more basic.
AspC159191macie:sideChainAsp 159 binds water and makes it more basic.

Literature References

Notes:
Müller JJ
Adrenodoxin reductase-adrenodoxin complex structure suggests electron transfer path in steroid biosynthesis.
J Biol Chem 2001 276 2786-2789
PubMed: 11053423
Beilke D
A new electron transport mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of adrenodoxin.
Biochemistry 2002 41 7969-7978
PubMed: 12069587
Ziegler GA
Crystal structures of adrenodoxin reductase in complex with NADP+ and NADPH suggesting a mechanism for the electron transfer of an enzyme family.
Biochemistry 2000 39 10986-10995
PubMed: 10998235
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