1J80

Osmolyte Stabilization of RNase

1J80 の概要

• エントリーDOI: 10.2210/pdb1j80/pdb
• 関連するPDBエントリー: 1J7Z
• 分子名称: RIBONUCLEASE PANCREATIC, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: osmolyte soaking, sarcosine, trimethylamine-n-oxide, betaine, taurine, hydrolase
• 由来する生物種: Bos taurus (cattle); 詳細
• 細胞内の位置: Secreted: P61823 P61823
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 13403.00

構造登録者

Ratnaparkhi, G.S.,Varadarajan, R. (登録日: 2001-05-19, 公開日: 2001-06-06, 最終更新日: 2024-10-30)

主引用文献

Ratnaparkhi, G.S.,Varadarajan, R.
Osmolytes stabilize ribonuclease S by stabilizing its fragments S protein and S peptide to compact folding-competent states.
J.Biol.Chem., 276:28789-28798, 2001

PubMed Abstract: Osmolytes stabilize proteins to thermal and chemical denaturation. We have studied the effects of the osmolytes sarcosine, betaine, trimethylamine-N-oxide, and taurine on the structure and stability of the protein.peptide complex RNase S using x-ray crystallography and titration calorimetry, respectively. The largest degree of stabilization is achieved with 6 m sarcosine, which increases the denaturation temperatures of RNase S and S pro by 24.6 and 17.4 degrees C, respectively, at pH 5 and protects both proteins against tryptic cleavage. Four crystal structures of RNase S in the presence of different osmolytes do not offer any evidence for osmolyte binding to the folded state of the protein or any perturbation in the water structure surrounding the protein. The degree of stabilization in 6 m sarcosine increases with temperature, ranging from -0.52 kcal mol(-1) at 20 degrees C to -5.4 kcal mol(-1) at 60 degrees C. The data support the thesis that osmolytes that stabilize proteins, do so by perturbing unfolded states, which change conformation to a compact, folding competent state in the presence of osmolyte. The increased stabilization thus results from a decrease in conformational entropy of the unfolded state.

PubMed: 11373282
DOI: 10.1074/jbc.M101906200

実験手法

X-RAY DIFFRACTION (2.1 Å)