Acta Crystallographica Section D Biological Crystallography · 2003 · 20 citations · 14 references
Crystal StructureProtein AssemblyBiomolecular Structure PredictionMolecular BiologyEscherichia ColiConserved Coa-binding ProteinHypothetical ProteinProtein FoldingProtein X-ray CrystallographyStructure-function Enzyme KineticsMulti-protein AssemblyProtein ChemistryProtein FunctionBiochemistryStructural BiologyNatural SciencesCell-free SystemCellular BiochemistryMedicine
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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