1IOT

STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATION

1IOT の概要

• エントリーDOI: 10.2210/pdb1iot/pdb
• 関連するPDBエントリー: 1IOQ 1IOR 1IOS
• 分子名称: LYSOZYME C (2 entities in total)
• 機能のキーワード: hydrolase, glycosidase, bacteriolytic enzyme
• 由来する生物種: Gallus gallus (chicken)
• 細胞内の位置: Secreted: P00698
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14313.12

構造登録者

Ohmura, T.,Ueda, T.,Ootsuka, K.,Saito, M.,Imoto, T. (登録日: 2001-03-28, 公開日: 2001-04-11, 最終更新日: 2024-11-06)

主引用文献

Ohmura, T.,Ueda, T.,Ootsuka, K.,Saito, M.,Imoto, T.
Stabilization of hen egg white lysozyme by a cavity-filling mutation.
Protein Sci., 10:313-320, 2001

PubMed Abstract: Stabilization of a protein using cavity-filling strategy has hardly been successful because of unfavorable van der Waals contacts. We succeeded in stabilizing lysozymes by cavity-filling mutations. The mutations were checked by a simple energy minimization in advance. It was shown clearly that the sum of free energy change caused by the hydrophobicity and the cavity size was correlated very well with protein stability. We also considered the aromatic-aromatic interaction. It is reconfirmed that the cavity-filling mutation in a hydrophobic core is a very useful method to stabilize a protein when the mutation candidate is selected carefully.

PubMed: 11266617
DOI: 10.1110/ps.37401

実験手法

X-RAY DIFFRACTION (1.75 Å)