2Z2E

Crystal Structure of Canine Milk Lysozyme Stabilized against Non-enzymatic Deamidation

2Z2E の概要

• エントリーDOI: 10.2210/pdb2z2e/pdb
• 分子名称: Lysozyme C, milk isozyme, SULFATE ION (3 entities in total)
• 機能のキーワード: lysozyme c, milk lysozyme, 1, 4-beta-n-acetylmuramidase c, bacteriolytic enzyme, hydrolase
• 由来する生物種: Canis lupus familiaris (dog)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29313.27

構造登録者

Nonaka, Y.,Akieda, D.,Watanabe, N.,Tanaka, I.,Kamiya, M.,Aizawa, T.,Nitta, K.,Demura, M.,Kawano, K. (登録日: 2007-05-21, 公開日: 2007-11-27, 最終更新日: 2024-11-06)

主引用文献

Nonaka, Y.,Aizawa, T.,Akieda, D.,Yasui, M.,Watanabe, M.,Watanabe, N.,Tanaka, I.,Kamiya, M.,Mizuguchi, M.,Demura, M.,Kawano, K.
Spontaneous asparaginyl deamidation of canine milk lysozyme under mild conditions
Proteins, 72:313-322, 2008

PubMed Abstract: Asparaginyl deamidation is a common form of nonenzymatic degradation of proteins and peptides. As it introduces a negative charge spontaneously and irreversibly, charge heterogeneity can be accumulated in protein solution during purification, preservation, and experiments. In this study, canine milk lysozyme (CML), a useful model for the study of the molten globule state, exhibited charge heterogeneity after sample purification. Four Asn residues in CML deamidated rapidly under mild conditions: pH 8.0 and 30 degrees C. Other than these residues, one Asn residue, which was stable in the native state, was labile to deamidation in the unfolded state. This suggests that the structural formation around Asn can suppress deamidation. Substitutions of these labile Asn residues to Gln residues prevented deamidation effectively. Because the substitutions did not disrupt the structural formation of the native and molten globule states, they will enable more precise analyses for physical and structural studies.

PubMed: 18214981
DOI: 10.1002/prot.21927

実験手法

X-RAY DIFFRACTION (2.01 Å)