2ZCZ

Crystal structures and thermostability of mutant TRAP3 A7 (ENGINEERED TRAP)

2ZCZ の概要

• エントリーDOI: 10.2210/pdb2zcz/pdb
• 関連するPDBエントリー: 1QAW 2EXS 2EXT 2ZD0
• 分子名称: Transcription attenuation protein mtrB, TRYPTOPHAN (3 entities in total)
• 機能のキーワード: linker, artificial, engineered, ring protein, 12-mer, rna-binding, transcription, transcription regulation, rna binding protein
• 由来する生物種: Geobacillus stearothermophilus
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 53754.87

構造登録者

Watanabe, M.,Mishima, Y.,Yamashita, I.,Park, S.Y.,Tame, J.R.H.,Heddle, J.G. (登録日: 2007-11-15, 公開日: 2008-04-29, 最終更新日: 2023-11-01)

主引用文献

Watanabe, M.,Mishima, Y.,Yamashita, I.,Park, S.Y.,Tame, J.R.,Heddle, J.G.
Intersubunit linker length as a modifier of protein stability: crystal structures and thermostability of mutant TRAP.
Protein Sci., 17:518-526, 2008

PubMed Abstract: The ability of proteins to self-assemble into complex, functional nanoscale structures is expected to become of significant use in the manufacture of artificial nanodevices with a wide range of novel applications. The bacterial protein TRAP has potential uses as a nanoscale component as it is ring-shaped, with a central, modifiable cavity. Furthermore, it can be engineered to make a ring of 12-fold symmetry, which is advantageous for packing into two-dimensional arrays. The 12mer form of TRAP is made by linking multiple subunits together on the same polypeptide, but the usefulness of the 12mers described to date is limited by their poor stability. Here we show that, by altering the length of the peptide linker between subunits, the thermostability can be significantly improved. Since the subunit interfaces of the different 12mers are essentially identical, stabilization arises from the reduction of strain in the linkers. Such a simple method of controlling the stability of modular proteins may have wide applications, and demonstrates the lack of absolute correlation between interactions observable by crystallography and the internal energy of a complex.

PubMed: 18287284
DOI: 10.1110/ps.073059308

実験手法

X-RAY DIFFRACTION (1.8 Å)