3ALY

Crystal Structure of RNase HI from Sulfolobus tokodaii with C-terminal deletion

3ALY の概要

• エントリーDOI: 10.2210/pdb3aly/pdb
• 関連するPDBエントリー: 2ehg
• 分子名称: Putative uncharacterized protein ST0753 (2 entities in total)
• 機能のキーワード: thermostable rnase hi, c-terminal anchor deletion, hydrolase
• 由来する生物種: Sulfolobus tokodaii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32470.11

構造登録者

Angkawidjaja, C.,Takano, K.,Kanaya, S. (登録日: 2010-08-10, 公開日: 2011-06-22, 最終更新日: 2023-11-01)

主引用文献

Takano, K.,Okamoto, T.,Okada, J.,Tanaka, S.,Angkawidjaja, C.,Koga, Y.,Kanaya, S.
Stabilization by fusion to the C-terminus of hyperthermophile Sulfolobus tokodaii RNase HI: a possibility of protein stabilization tag
Plos One, 6:e16226-e16226, 2011

PubMed Abstract: RNase HI from the hyperthermophile Sulfolobus tokodaii (Sto-RNase HI) is stabilized by its C-terminal residues. In this work, the stabilization effect of the Sto-RNase HI C-terminal residues was investigated in detail by thermodynamic measurements of the stability of variants lacking the disulfide bond (C58/145A), or the six C-terminal residues (ΔC6) and by structural analysis of ΔC6. The results showed that the C-terminal does not affect overall structure and stabilization is caused by local interactions of the C-terminal, suggesting that the C-terminal residues could be used as a "stabilization tag." The Sto-RNase HI C-terminal residues (-IGCIILT) were introduced as a tag on three proteins. Each chimeric protein was more stable than its wild-type protein. These results suggested the possibility of a simple stabilization technique using a stabilization tag such as Sto-RNase HI C-terminal residues.

PubMed: 21283826
DOI: 10.1371/journal.pone.0016226

実験手法

X-RAY DIFFRACTION (1.66 Å)