1l6u: Difference between revisions

Revision as of 11:49, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1l6u.png

Template:STRUCTURE 1l6u

NMR STRUCTURE OF OXIDIZED ADRENODOXINNMR STRUCTURE OF OXIDIZED ADRENODOXIN

Template:ABSTRACT PUBMED 12069587

About this StructureAbout this Structure

1L6U is a Single protein structure of sequence from Bos taurus. Full experimental 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

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 {{STRUCTURE_1l6u|  PDB=1l6u  |  SCENE=  }}
-'''NMR STRUCTURE OF OXIDIZED ADRENODOXIN'''
+===NMR STRUCTURE OF OXIDIZED 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12069587}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12069587 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12069587}}
 ==About this Structure==
-L6U 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=1L6U OCA].
+L6U is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L6U OCA].
 ==Reference==
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