1iuk
From Proteopedia
(New page: 200px<br /><applet load="1iuk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iuk, resolution 1.70Å" /> '''The structure of nat...) |
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- | [[Image:1iuk.gif|left|200px]]<br /><applet load="1iuk" size=" | + | [[Image:1iuk.gif|left|200px]]<br /><applet load="1iuk" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1iuk, resolution 1.70Å" /> | caption="1iuk, resolution 1.70Å" /> | ||
'''The structure of native ID.343 from Thermus thermophilus'''<br /> | '''The structure of native ID.343 from Thermus thermophilus'''<br /> | ||
==Overview== | ==Overview== | ||
- | TT1466 is a hypothetical protein from the extremely thermophilic bacterium | + | 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== | ||
- | 1IUK 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:// | + | 1IUK 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=1IUK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
[[Category: Kuramitsu, S.]] | [[Category: Kuramitsu, S.]] | ||
- | [[Category: Park, S | + | [[Category: Park, S Y.]] |
- | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Shirouzu, M.]] | [[Category: Shirouzu, M.]] | ||
- | [[Category: Tame, J | + | [[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]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:15:49 2008'' |
Revision as of 11:15, 21 February 2008
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The structure of native ID.343 from Thermus thermophilus
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.
About this Structure
1IUK is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
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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