1iul: Difference between revisions

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New page: left|200px<br /><applet load="1iul" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iul, resolution 2.0Å" /> '''The structure of cell...
 
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[[Image:1iul.gif|left|200px]]<br /><applet load="1iul" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1iul.gif|left|200px]]<br /><applet load="1iul" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1iul, resolution 2.0&Aring;" />
caption="1iul, resolution 2.0&Aring;" />
'''The structure of cell-free ID.343 from Thermus thermophilus'''<br />
'''The structure of cell-free ID.343 from Thermus thermophilus'''<br />


==Overview==
==Overview==
TT1466 is a hypothetical protein from the extremely thermophilic bacterium, Thermus thermophilus HB8 and is highly conserved in bacteria and archaea., The selenomethionyl protein was synthesized by a cell-free system and the, crystal structure was determined at 2.0 A by MAD phasing. A native crystal, was used for structure refinement to 1.7 A. The structure is highly, homologous to that of the CoA-binding domain of the succinyl-CoA, synthetase from Escherichia coli, despite the protein having only 14%, sequence identity to this domain. An isothermal titration calorimetry, experiment was performed to investigate whether TT1466 binds CoA and, revealed high-affinity CoA binding of TT1466.
TT1466 is a hypothetical protein from the extremely thermophilic bacterium Thermus thermophilus HB8 and is highly conserved in bacteria and archaea. The selenomethionyl protein was synthesized by a cell-free system and the crystal structure was determined at 2.0 A by MAD phasing. A native crystal was used for structure refinement to 1.7 A. The structure is highly homologous to that of the CoA-binding domain of the succinyl-CoA synthetase from Escherichia coli, despite the protein having only 14% sequence identity to this domain. An isothermal titration calorimetry experiment was performed to investigate whether TT1466 binds CoA and revealed high-affinity CoA binding of TT1466.


==About this Structure==
==About this Structure==
1IUL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IUL OCA].  
1IUL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IUL OCA].  


==Reference==
==Reference==
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[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
[[Category: Kuramitsu, S.]]
[[Category: Kuramitsu, S.]]
[[Category: Park, S.Y.]]
[[Category: Park, S Y.]]
[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Shirouzu, M.]]
[[Category: Shirouzu, M.]]
[[Category: Tame, J.R.]]
[[Category: Tame, J R.]]
[[Category: Wada, T.]]
[[Category: Wada, T.]]
[[Category: Yokoyama, S.]]
[[Category: Yokoyama, S.]]
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[[Category: structural genomics]]
[[Category: structural genomics]]


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Revision as of 14:15, 21 February 2008

File:1iul.gif


1iul, resolution 2.0Å

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The structure of cell-free ID.343 from Thermus thermophilus

OverviewOverview

TT1466 is a hypothetical protein from the extremely thermophilic bacterium Thermus thermophilus HB8 and is highly conserved in bacteria and archaea. The selenomethionyl protein was synthesized by a cell-free system and the crystal structure was determined at 2.0 A by MAD phasing. A native crystal was used for structure refinement to 1.7 A. The structure is highly homologous to that of the CoA-binding domain of the succinyl-CoA synthetase from Escherichia coli, despite the protein having only 14% sequence identity to this domain. An isothermal titration calorimetry experiment was performed to investigate whether TT1466 binds CoA and revealed high-affinity CoA binding of TT1466.

About this StructureAbout this Structure

1IUL is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of a conserved CoA-binding protein synthesized by a cell-free system., Wada T, Shirouzu M, Terada T, Ishizuka Y, Matsuda T, Kigawa T, Kuramitsu S, Park SY, Tame JR, Yokoyama S, Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1213-8. Epub 2003, Jun 27. PMID:12832765

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