1IUK
The structure of native ID.343 from Thermus thermophilus
Summary for 1IUK
| Entry DOI | 10.2210/pdb1iuk/pdb |
| Related | 1IUL |
| Descriptor | hypothetical protein TT1466 (2 entities in total) |
| Functional Keywords | structural genomics, riken structural genomics/proteomics initiative, rsgi, unknown function |
| Biological source | Thermus thermophilus |
| Total number of polymer chains | 1 |
| Total formula weight | 15889.45 |
| Authors | Wada, T.,Shirouzu, M.,Park, S.-Y.,Tame, J.R.,Kuramitsu, S.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2002-03-05, release date: 2003-07-15, Last modification date: 2023-10-25) |
| Primary citation | Wada, T.,Shirouzu, M.,Terada, T.,Ishizuka, Y.,Matsuda, T.,Kigawa, T.,Kuramitsu, S.,Park, S.Y.,Tame, J.R.,Yokoyama, S. Structure of a conserved CoA-binding protein synthesized by a cell-free system. Acta Crystallogr.,Sect.D, 59:1213-1218, 2003 Cited by PubMed Abstract: 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. PubMed: 12832765DOI: 10.1107/S0907444903010515 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
Download full validation report
