1ayf
From Proteopedia
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|PDB= 1ayf |SIZE=350|CAPTION= <scene name='initialview01'>1ayf</scene>, resolution 1.85Å | |PDB= 1ayf |SIZE=350|CAPTION= <scene name='initialview01'>1ayf</scene>, resolution 1.85Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene> | + | |LIGAND= <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ayf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ayf OCA], [http://www.ebi.ac.uk/pdbsum/1ayf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ayf RCSB]</span> | ||
}} | }} | ||
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[[Category: Mueller, A.]] | [[Category: Mueller, A.]] | ||
[[Category: Mueller, J J.]] | [[Category: Mueller, J J.]] | ||
| - | [[Category: FES]] | ||
| - | [[Category: GOL]] | ||
[[Category: [2fe-2s]ferredoxin]] | [[Category: [2fe-2s]ferredoxin]] | ||
[[Category: adrenodoxin]] | [[Category: adrenodoxin]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:49:57 2008'' |
Revision as of 15:49, 30 March 2008
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| , resolution 1.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BOVINE ADRENODOXIN (OXIDIZED)
Overview
BACKGROUND: Adrenodoxin (Adx) is a [2Fe-2S] ferredoxin involved in steroid hormone biosynthesis in the adrenal gland mitochondrial matrix of mammals. Adx is a small soluble protein that transfers electrons from adrenodoxin reductase (AR) to different cytochrome P450 isoforms where they are consumed in hydroxylation reactions. A crystallographic study of Adx is expected to reveal the structural basis for an important electron transfer reaction mediated by a vertebrate [2Fe-2S] ferredoxin. RESULTS: The crystal structure of a truncated bovine adrenodoxin, Adx(4-108), was determined at 1.85 A resolution and refined to a crystallographic R value of 0.195. The structure was determined using multiple wavelength anomalous dispersion phasing techniques, making use of the iron atoms in the [2Fe-2S] cluster of the protein. The protein displays the compact (alpha + beta) fold typical for [2Fe-2S] ferredoxins. The polypeptide chain is organized into a large core domain and a smaller interaction domain which comprises 35 residues, including all those previously determined to be involved in binding to AR and cytochrome P450. A small interdomain motion is observed as a structural difference between the two independent molecules in the asymmetric unit of the crystal. Charged residues of Adx(4-108) are clustered to yield a strikingly asymmetric electric potential of the protein molecule. CONCLUSIONS: The crystal structure of Adx(4-108) provides the first detailed description of a vertebrate [2Fe-2S] ferredoxin and serves to explain a large body of biochemical studies in terms of a three-dimensional structure. The structure suggests how a change in the redox state of the [2Fe-2S] cluster may be coupled to a domain motion of the protein. It seems likely that the clearly asymmetric charge distribution on the surface of Adx(4-108) and the resulting strong molecular dipole are involved in electrostatic steering of the interactions with AR and cytochrome P450.
About this Structure
1AYF is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx(4-108)., Muller A, Muller JJ, Muller YA, Uhlmann H, Bernhardt R, Heinemann U, Structure. 1998 Mar 15;6(3):269-80. PMID:9551550[[Category: [2fe-2s]ferredoxin]]
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