1CJR

X-RAY CRYSTALLOGRAPHIC STUDIES OF DENATURATION IN RIBONUCLEASE S

1CJR の概要

• エントリーDOI: 10.2210/pdb1cjr/pdb
• 分子名称: PROTEIN (RIBONUCLEASE S), SULFATE ION, ... (4 entities in total)
• 機能のキーワード: rnase, crosslinking, low ph, denaturation, hydrolase
• 由来する生物種: synthetic construct; 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: 13143.76

構造登録者

Ratnaparkhi, G.S.,Varadarajan, R. (登録日: 1999-04-19, 公開日: 1999-05-07, 最終更新日: 2024-10-30)

主引用文献

Ratnaparkhi, G.S.,Varadarajan, R.
X-ray crystallographic studies of the denaturation of ribonuclease S.
Proteins, 36:282-294, 1999

PubMed Abstract: In an attempt to view the onset of urea denaturation in ribonuclease we have collected X-ray diffraction data on ribonuclease S crystals soaked in 0, 1.5, 2, 3, and 5 molar urea. At concentrations above 2 M urea, crystals were stabilized by glutaraldehyde crosslinking. We have also collected data on ribonuclease S crystals at low pH in an attempt to study the onset of pH denaturation. The resolution of the datasets range from 1.9 to 3.0 A. Analysis of the structures reveals an increase in disorder with increasing urea concentration. In the 5 M urea structure, this increase in disorder is apparent all over the structure but is larger in loop and helical regions than in the beta strands. The low pH structure shows a very similar pattern of increased disorder. In addition there is a major change in the position of the main chain (> 1 A) in the 65-72 turn region. This region has previously been shown to be involved in one of the initial steps of unfolding in the reduction of ribonuclease A. Crystallographic analyses in the presence of denaturant, when combined with controlled crosslinking, can thus provide detailed structural information that is related to the initial steps of unfolding in solution. Proteins 1999;36:282-294.

PubMed: 10409822
DOI: 10.1002/(SICI)1097-0134(19990815)36:3<282::AID-PROT3>3.3.CO;2-6

実験手法

X-RAY DIFFRACTION (2.3 Å)