1IUK

The structure of native ID.343 from Thermus thermophilus

1IUK の概要

• エントリーDOI: 10.2210/pdb1iuk/pdb
• 関連するPDBエントリー: 1IUL
• 分子名称: hypothetical protein TT1466 (2 entities in total)
• 機能のキーワード: structural genomics, riken structural genomics/proteomics initiative, rsgi, unknown function
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15889.45

構造登録者

Wada, T.,Shirouzu, M.,Park, S.-Y.,Tame, J.R.,Kuramitsu, S.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2002-03-05, 公開日: 2003-07-15, 最終更新日: 2023-10-25)

主引用文献

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

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: 12832765
DOI: 10.1107/S0907444903010515

実験手法

X-RAY DIFFRACTION (1.7 Å)