1l6u

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Revision as of 21:12, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1l6u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l6u" /> '''NMR STRUCTURE OF OXIDIZED ADRENODOXIN'''<br ...)
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1l6u

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NMR STRUCTURE OF OXIDIZED ADRENODOXIN

OverviewOverview

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 StructureAbout this Structure

1L6U is a Single protein structure of sequence from Bos taurus with FES as ligand. Full crystallographic information is available from OCA.

ReferenceReference

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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