3WW6

Crystal Structure of hen egg white lysozyme mutant N46D/D52S

3WW6 の概要

• エントリーDOI: 10.2210/pdb3ww6/pdb
• 関連するPDBエントリー: 2lzt 3ww5
• 分子名称: Lysozyme C, CHLORIDE ION (3 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Gallus gallus (bantam,chickens)
• 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: 14481.40

構造登録者

Abe, Y.,Kubota, M.,Ito, Y.,Imoto, T.,Ueda, T. (登録日: 2014-06-17, 公開日: 2015-06-17, 最終更新日: 2024-10-16)

主引用文献

Abe, Y.,Kubota, M.,Takazaki, S.,Ito, Y.,Yamamoto, H.,Kang, D.,Ueda, T.,Imoto, T.
Effect on catalysis by replacement of catalytic residue from hen egg white lysozyme to Venerupis philippinarum lysozyme.
Protein Sci., 25:1637-1647, 2016

PubMed Abstract: Asn46Asp/Asp52Ser or Asn46Glu/Asp52Ser hen egg white lysozyme (HEL) mutant was designed by introducing the substituted catalytic residue Asp46 or Glu46, respectively, based on Venerupis philippinarum (Vp) lysozyme structure as a representative of invertebrate-type (i-type) lyzozyme. These mutations restored the bell-shaped pH-dependency of the enzyme activity from the sigmoidal pH-dependency observed for the Asp52Ser mutant. Furthermore both lysozyme mutants possessed retaining mechanisms like Vp lysozyme and HEL. The Asn46Glu/Asp52Ser mutant, which has a shorter distance between two catalytic residues, formed a glycosyl adduct in the reaction with the N-acetylglucosamine oligomer. Furthermore, we found the accelerated turnover through its glycosyl adduct formation and decomposition. The turnover rate estimated from the glycosyl formation and decomposition rates was only 20% of the observed hydrolysis rate of the substrate. Based on these results, we discussed the catalytic mechanism of lysozymes.

PubMed: 27291073
DOI: 10.1002/pro.2966

実験手法

X-RAY DIFFRACTION (1.53 Å)