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| - | [[Image:1ayf.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1ayf| PDB=1ayf | SCENE= }} | | {{STRUCTURE_1ayf| PDB=1ayf | SCENE= }} |
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| - | '''BOVINE ADRENODOXIN (OXIDIZED)'''
| + | ===BOVINE ADRENODOXIN (OXIDIZED)=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9551550}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9551550 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9551550}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Adrenodoxin]] | | [[Category: Adrenodoxin]] |
| | [[Category: Electron transport]] | | [[Category: Electron transport]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:50:41 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:51:34 2008'' |
Revision as of 14:51, 30 June 2008
Template:STRUCTURE 1ayf
BOVINE ADRENODOXIN (OXIDIZED)
Template:ABSTRACT PUBMED 9551550
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
Page seeded by OCA on Mon Jun 30 17:51:34 2008
