1JL1

D10A E. coli ribonuclease HI

1JL1 の概要

• エントリーDOI: 10.2210/pdb1jl1/pdb
• 関連するPDBエントリー: 1F21
• 分子名称: RIBONUCLEASE HI (2 entities in total)
• 機能のキーワード: rnase hi, protein stability, thermostability, hydrogen exchange, cooperativity, hydrolase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm (Potential): P0A7Y4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17482.79

構造登録者

Goedken, E.R.,Marqusee, S. (登録日: 2001-07-13, 公開日: 2002-02-27, 最終更新日: 2023-08-16)

主引用文献

Goedken, E.R.,Marqusee, S.
Native-state energetics of a thermostabilized variant of ribonuclease HI.
J.Mol.Biol., 314:863-871, 2001

PubMed Abstract: Escherichia coli RNase HI is a well-characterized model system for protein folding and stability. Controlling protein stability is critical for both natural proteins and for the development of engineered proteins that function under extreme conditions. We have used native-state hydrogen exchange on a variant containing the stabilizing mutation Asp10 to alanine in order to determine its residue-specific stabilities. On average, the DeltaG(unf) value for each residue was increased by 2-3 kcal/mol, resulting in a lower relative population of partially unfolded forms. Though increased in stability by a uniform factor, D10A shows a distribution of stabilities in its secondary structural units that is similar to that of E. coli RNase H, but not the closely related protein from Thermus thermophilus. Hence, the simple mutation used to stabilize the enzyme does not recreate the balance of conformational flexibility evolved in the thermophilic protein.

PubMed: 11734003
DOI: 10.1006/jmbi.2001.5184

実験手法

X-RAY DIFFRACTION (1.3 Å)