3DIB

Crystal structure of bovine pancreatic ribonuclease A variant (I106A)

3DIB の概要

• エントリーDOI: 10.2210/pdb3dib/pdb
• 関連するPDBエントリー: 3DH5 3DH6 3DI7 3DI8 3DI9 3DIC
• 分子名称: Ribonuclease pancreatic, CHLORIDE ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: ribonuclease, rnase a, hydrolase, bovine pancreas, endonuclease, glycation, glycoprotein, nuclease, secreted
• 由来する生物種: Bos taurus (bovine)
• 細胞内の位置: Secreted: P61823
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13939.57

構造登録者

Kurpiewska, K.,Font, J.,Ribo, M.,Vilanova, M.,Lewinski, K. (登録日: 2008-06-20, 公開日: 2008-07-15, 最終更新日: 2024-10-30)

主引用文献

Kurpiewska, K.,Font, J.,Ribo, M.,Vilanova, M.,Lewinski, K.
X-ray crystallographic studies of RNase A variants engineered at the most destabilizing positions of the main hydrophobic core: further insight into protein stability
Proteins, 77:658-669, 2009

PubMed Abstract: To investigate the structural origin of decreased pressure and temperature stability, the crystal structure of bovine pancreatic ribonuclease A variants V47A, V54A, V57A, I81A, I106A, and V108A was solved at 1.4-2.0 A resolution and compared with the structure of wild-type protein. The introduced mutations had only minor influence on the global structure of ribonuclease A. The structural changes had individual character that depends on the localization of mutated residue, however, they seemed to expand from mutation site to the rest of the structure. Several different parameters have been evaluated to find correlation with decrease of free energy of unfolding DeltaDeltaG(T), and the most significant correlation was found for main cavity volume change. Analysis of the difference distance matrices revealed that the ribonuclease A molecule is organized into five relatively rigid subdomains with individual response to mutation. This behavior consistent with results of unfolding experiments is an intrinsic feature of ribonuclease A that might be surviving remnants of folding intermediates and reflects the dynamic nature of the molecule.

PubMed: 19544568
DOI: 10.1002/prot.22480

実験手法

X-RAY DIFFRACTION (1.4 Å)