2b5x
From Proteopedia
(New page: 200px<br /><applet load="2b5x" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b5x" /> '''Solution Structure of a Thioredoxin-like Pro...) |
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| - | [[Image:2b5x.gif|left|200px]]<br /><applet load="2b5x" size=" | + | [[Image:2b5x.gif|left|200px]]<br /><applet load="2b5x" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''Solution Structure of a Thioredoxin-like Protein in the Reduced Form'''<br /> | '''Solution Structure of a Thioredoxin-like Protein in the Reduced Form'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Bacillus subtilis YkuV responds to environmental oxidative stress and | + | The Bacillus subtilis YkuV responds to environmental oxidative stress and plays an important role for the bacteria to adapt to the environment. Bioinformatic analysis suggests that YkuV is a homolog of membrane-anchored proteins and belongs to the thioredoxin-like protein superfamily containing the typical Cys-Xaa-Xaa-Cys active motif. However, the biological function of this protein remains unknown thus far. In order to elucidate the biological function, we have determined the solution structures of both the oxidized and reduced forms of B. subtilis YkuV by NMR spectroscopy and performed biochemical studies. Our results demonstrated that the reduced YkuV has a low midpoint redox potential, allowing it to reduce a variety of protein substrates. The overall structures of both oxidized and reduced forms are similar, with a typical thioredoxin-like fold. However, significant conformational changes in the Cys-Xaa-Xaa-Cys active motif of the tertiary structures are observed between the two forms. In addition, the backbone dynamics provide further insights in understanding the strong redox potential of the reduced YkuV. Furthermore, we demonstrated that YkuV is able to reduce different protein substrates in vitro. Together, our results clearly established that YkuV may function as a general thiol:disulfide oxidoreductase, which acts as an alternative for thioredoxin or thioredoxin reductase to maintain the reducing environment in the cell cytoplasm. |
==About this Structure== | ==About this Structure== | ||
| - | 2B5X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http:// | + | 2B5X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B5X OCA]. |
==Reference== | ==Reference== | ||
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[[Category: thioredoxin-like]] | [[Category: thioredoxin-like]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:34:31 2008'' |
Revision as of 14:34, 21 February 2008
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Solution Structure of a Thioredoxin-like Protein in the Reduced Form
Overview
The Bacillus subtilis YkuV responds to environmental oxidative stress and plays an important role for the bacteria to adapt to the environment. Bioinformatic analysis suggests that YkuV is a homolog of membrane-anchored proteins and belongs to the thioredoxin-like protein superfamily containing the typical Cys-Xaa-Xaa-Cys active motif. However, the biological function of this protein remains unknown thus far. In order to elucidate the biological function, we have determined the solution structures of both the oxidized and reduced forms of B. subtilis YkuV by NMR spectroscopy and performed biochemical studies. Our results demonstrated that the reduced YkuV has a low midpoint redox potential, allowing it to reduce a variety of protein substrates. The overall structures of both oxidized and reduced forms are similar, with a typical thioredoxin-like fold. However, significant conformational changes in the Cys-Xaa-Xaa-Cys active motif of the tertiary structures are observed between the two forms. In addition, the backbone dynamics provide further insights in understanding the strong redox potential of the reduced YkuV. Furthermore, we demonstrated that YkuV is able to reduce different protein substrates in vitro. Together, our results clearly established that YkuV may function as a general thiol:disulfide oxidoreductase, which acts as an alternative for thioredoxin or thioredoxin reductase to maintain the reducing environment in the cell cytoplasm.
About this Structure
2B5X is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
The Bacillus subtilis YkuV is a thiol:disulfide oxidoreductase revealed by its redox structures and activity., Zhang X, Hu Y, Guo X, Lescop E, Li Y, Xia B, Jin C, J Biol Chem. 2006 Mar 24;281(12):8296-304. Epub 2006 Jan 17. PMID:16418167
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