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1iul

From Proteopedia

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{{STRUCTURE_1iul| PDB=1iul | SCENE= }}
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'''The structure of cell-free ID.343 from Thermus thermophilus'''
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===The structure of cell-free ID.343 from Thermus thermophilus===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_12832765}}
==About this Structure==
==About this Structure==
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[[Category: Rsgi]]
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Revision as of 11:01, 1 July 2008

Image:1iul.png

Template:STRUCTURE 1iul

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

Template:ABSTRACT PUBMED 12832765

About this Structure

1IUL 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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