1L20

ENHANCED PROTEIN THERMOSTABILITY FROM DESIGNED MUTATIONS THAT INTERACT WITH ALPHA-HELIX DIPOLES

1L20 の概要

• エントリーDOI: 10.2210/pdb1l20/pdb
• 関連するPDBエントリー: 1L01 1L02 1L03 1L04 1L05 1L06 1L07 1L08 1L09 1L10 1L11 1L12 1L13 1L14 1L15 1L16 1L17 1L18 1L19 1L21 1L22 1L23 1L24 1L25 1L26 1L27 1L28 1L29 1L30 1L31 1L32 1L33 1L34 1L35 1L36 2LZM
• 分子名称: T4 LYSOZYME (2 entities in total)
• 機能のキーワード: hydrolase (o-glycosyl)
• 由来する生物種: Enterobacteria phage T4
• 細胞内の位置: Host cytoplasm : P00720
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18663.45

構造登録者

Nicholson, H.,Matthews, B.W. (登録日: 1989-05-01, 公開日: 1990-01-15, 最終更新日: 2024-05-22)

主引用文献

Nicholson, H.,Becktel, W.J.,Matthews, B.W.
Enhanced protein thermostability from designed mutations that interact with alpha-helix dipoles.
Nature, 336:651-656, 1988

PubMed Abstract: Two different genetically engineered amino-acid substitutions designed to interact with alpha-helix dipoles in T4 lysozyme are shown to increase the thermal stability of the protein. Crystallographic analyses of the mutant lysozyme structures suggest that the stabilization is due to electrostatic interaction and does not require precise hydrogen bonding between the substituted amino acid and the end of the alpha-helix.

PubMed: 3200317
DOI: 10.1038/336651a0

実験手法

X-RAY DIFFRACTION (1.85 Å)