1l6v

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[[Image:1l6v.jpg|left|200px]]<br /><applet load="1l6v" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1l6v.jpg|left|200px]]
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caption="1l6v" />
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'''STRUCTURE OF REDUCED BOVINE ADRENODOXIN'''<br />
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{{Structure
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|PDB= 1l6v |SIZE=350|CAPTION= <scene name='initialview01'>1l6v</scene>
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|SITE=
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|LIGAND= <scene name='pdbligand=FES:FE2/S2 (INORGANIC) CLUSTER'>FES</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''STRUCTURE OF REDUCED BOVINE ADRENODOXIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1L6V 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> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L6V OCA].
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1L6V is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L6V OCA].
==Reference==
==Reference==
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A new electron transport mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of adrenodoxin., Beilke D, Weiss R, Lohr F, Pristovsek P, Hannemann F, Bernhardt R, Ruterjans H, Biochemistry. 2002 Jun 25;41(25):7969-78. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12069587 12069587]
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A new electron transport mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of adrenodoxin., Beilke D, Weiss R, Lohr F, Pristovsek P, Hannemann F, Bernhardt R, Ruterjans H, Biochemistry. 2002 Jun 25;41(25):7969-78. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12069587 12069587]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Weiss, R.]]
[[Category: Weiss, R.]]
[[Category: FES]]
[[Category: FES]]
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[[Category: 5 beta strands]]
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[[Category: 5 beta strand]]
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[[Category: 5 helices]]
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[[Category: 5 helice]]
[[Category: [2fe-2s]-cluster]]
[[Category: [2fe-2s]-cluster]]
[[Category: primary interaction domain (helix 72-79)]]
[[Category: primary interaction domain (helix 72-79)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:41:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:27:11 2008''

Revision as of 10:27, 20 March 2008


PDB ID 1l6v

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Ligands:
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF REDUCED BOVINE ADRENODOXIN


Overview

The adrenal ferredoxin (adrenodoxin, Adx) is an acidic 14.4-kDa [2Fe-2S] ferredoxin that belongs to the vertebrate ferredoxin family. It is involved in the electron transfer from the flavoenzyme NADPH-adrenodoxin-reductase to cytochromes P-450(scc) and P-450(11)(beta). The interaction between the redox partners during electron transport has not yet been fully established. Determining the tertiary structure of an electron-transfer protein may be very helpful in understanding the transport mechanism. In the present work, we report a structural study on the oxidized and reduced forms of bovine adrenodoxin (bAdx) in solution using high-resolution NMR spectroscopy. The protein was produced in Escherichia coli and singly or doubly labeled with (15)N or (13)C/(15)N, respectively. Approximately 70 and 75% of the (15)N, (13)C, and (1)H resonances could be assigned for the reduced and the oxidized bAdx, respectively. The secondary and tertiary structures of the reduced and oxidized states were determined using NOE distance information. (1)H(N)-T(1) relaxation times of certain residues were used to obtain additional distance constraints to the [2Fe-2S] cluster. The results suggest that the solution structure of oxidized Adx is quite similar to the X-ray structure. However, structural changes occur upon reduction of the [2Fe-2S] cluster, as indicated by NMR measurements. It could be shown that these conformational changes, especially in the C-terminal region, cause the dissociation of the Adx dimer upon reduction. A new electron transport mechanism proceeding via a modified shuttle mechanism, with both monomers and dimers acting as electron carriers, is proposed.

About this Structure

1L6V is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

A new electron transport mechanism in mitochondrial steroid hydroxylase systems based on structural changes upon the reduction of adrenodoxin., Beilke D, Weiss R, Lohr F, Pristovsek P, Hannemann F, Bernhardt R, Ruterjans H, Biochemistry. 2002 Jun 25;41(25):7969-78. PMID:12069587[[Category: [2fe-2s]-cluster]]

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