structural genomics papers
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 Å by MAD phasing. A native crystal was used for structure refinement to 1.7 Å. 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.
Supporting information
PDB references: TT1466 from cell-free system, 1iul, r1iulsf; TT1466 expressed in E. coli, 1iuk, r1iuksf