1ayf
From Proteopedia
(New page: 200px<br /><applet load="1ayf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ayf, resolution 1.85Å" /> '''BOVINE ADRENODOXIN (...) |
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| - | [[Image:1ayf.gif|left|200px]]<br /><applet load="1ayf" size=" | + | [[Image:1ayf.gif|left|200px]]<br /><applet load="1ayf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ayf, resolution 1.85Å" /> | caption="1ayf, resolution 1.85Å" /> | ||
'''BOVINE ADRENODOXIN (OXIDIZED)'''<br /> | '''BOVINE ADRENODOXIN (OXIDIZED)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: Adrenodoxin (Adx) is a [2Fe-2S] ferredoxin involved in steroid | + | 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== | ==About this Structure== | ||
| - | 1AYF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with FES and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1AYF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=FES:'>FES</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AYF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Heinemann, U.]] | [[Category: Heinemann, U.]] | ||
[[Category: Mueller, A.]] | [[Category: Mueller, A.]] | ||
| - | [[Category: Mueller, J | + | [[Category: Mueller, J J.]] |
[[Category: FES]] | [[Category: FES]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
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[[Category: electron transport]] | [[Category: electron transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:49:34 2008'' |
Revision as of 09:49, 21 February 2008
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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 with and as ligands. 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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