1MP9

TBP from a mesothermophilic archaeon, Sulfolobus acidocaldarius

1MP9 の概要

• エントリーDOI: 10.2210/pdb1mp9/pdb
• 分子名称: TATA-binding protein (2 entities in total)
• 機能のキーワード: transcription regulation, dna-binding protein, transcription factor, dna binding protein
• 由来する生物種: Sulfolobus acidocaldarius
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 44996.66

構造登録者

Koike, H.,Kawashima-Ohya, Y.,Yamasaki, T.,Clowney, L.,Katsuya, Y.,Suzuki, M. (登録日: 2002-09-12, 公開日: 2003-11-04, 最終更新日: 2024-03-13)

主引用文献

Koike, H.,Kawashima-Ohya, Y.,Yamasaki, T.,Clowney, L.,Katsuya, Y.,Suzuki, M.
Origins of Protein Stability Revealed by Comparing Crystal Structures of TATA Binding Proteins.
Structure, 12:157-168, 2004

PubMed Abstract: The crystal structure of TATA binding protein (TBP) from a mesothermophilic archaeon, Sulfolobus acidocaldarius, has been determined at a resolution of 2.0 A with an R factor of 20.9%. By comparing this structure with the structures of TBPs from a hyperthermophilic archaeon and mesophilic eukaryotes, as well as by comparing amino acid sequences of TBPs from archaea, covering a wide range of optimum growth temperatures, two significant determinants of the stability of TBP have been identified: increasing the interior hydrophobicity by interaction between three residues, Val, Leu, and Ile, with further differentiation of the surface, and increasing its hydrophilicity and raising the cost of unfolding. These findings suggest directions along which the stability of TBP can be engineered.

PubMed: 14725775
DOI: 10.1016/j.str.2003.12.003

実験手法

X-RAY DIFFRACTION (2 Å)