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New page: left|200px<br /><applet load="1on4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1on4" /> '''Solution structure of soluble domain of Sco1...
 
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[[Image:1on4.jpg|left|200px]]<br /><applet load="1on4" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1on4.jpg|left|200px]]<br /><applet load="1on4" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1on4" />
caption="1on4" />
'''Solution structure of soluble domain of Sco1 from Bacillus Subtilis'''<br />
'''Solution structure of soluble domain of Sco1 from Bacillus Subtilis'''<br />


==Overview==
==Overview==
Sco1, a protein required for the proper assembly of cytochrome c oxidase, has a soluble domain anchored to the cytoplasmic membrane through a single, transmembrane segment. The solution structure of the soluble part of, apoSco1 from Bacillus subtilis has been solved by NMR and the internal, mobility characterized. Its fold places Sco1 in a distinct subgroup of the, functionally unrelated thioredoxin proteins. In vitro Sco1 binds copper(I), through a CXXXCP motif and possibly His 135 and copper(II) in two, different species, thus suggesting that copper(II) is adventitious more, than physiological. The Sco1 structure represents the first structure of, this class of proteins, present in a variety of eukaryotic and bacterial, organisms, and elucidates a link between copper trafficking proteins and, thioredoxins. The availability of the structure has allowed us to model, the homologs Sco1 and Sco2 from S. cerevisiae and to discuss the, physiological role of the Sco family.
Sco1, a protein required for the proper assembly of cytochrome c oxidase, has a soluble domain anchored to the cytoplasmic membrane through a single transmembrane segment. The solution structure of the soluble part of apoSco1 from Bacillus subtilis has been solved by NMR and the internal mobility characterized. Its fold places Sco1 in a distinct subgroup of the functionally unrelated thioredoxin proteins. In vitro Sco1 binds copper(I) through a CXXXCP motif and possibly His 135 and copper(II) in two different species, thus suggesting that copper(II) is adventitious more than physiological. The Sco1 structure represents the first structure of this class of proteins, present in a variety of eukaryotic and bacterial organisms, and elucidates a link between copper trafficking proteins and thioredoxins. The availability of the structure has allowed us to model the homologs Sco1 and Sco2 from S. cerevisiae and to discuss the physiological role of the Sco family.


==About this Structure==
==About this Structure==
1ON4 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ON4 OCA].  
1ON4 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=1ON4 OCA].  


==Reference==
==Reference==
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[[Category: Cantini, F.]]
[[Category: Cantini, F.]]
[[Category: Ciofi-Baffoni, S.]]
[[Category: Ciofi-Baffoni, S.]]
[[Category: SPINE, Structural.Proteomics.in.Europe.]]
[[Category: SPINE, Structural Proteomics in Europe.]]
[[Category: copper protein]]
[[Category: copper protein]]
[[Category: cox assembly protein]]
[[Category: cox assembly protein]]
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[[Category: ypmq]]
[[Category: ypmq]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:01:37 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:19:32 2008''