1KXY

ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE AND CHARGED SIDE CHAINS

1KXY の概要

• エントリーDOI: 10.2210/pdb1kxy/pdb
• 分子名称: LYSOZYME (2 entities in total)
• 機能のキーワード: hydrolase, glycosidase, electrostatic interaction, helix, hen lysozyme, stability
• 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: 14330.18

構造登録者

Motoshima, H.,Ohmura, T.,Ueda, T.,Imoto, T. (登録日: 1996-11-22, 公開日: 1997-11-26, 最終更新日: 2024-10-30)

主引用文献

Motoshima, H.,Mine, S.,Masumoto, K.,Abe, Y.,Iwashita, H.,Hashimoto, Y.,Chijiiwa, Y.,Ueda, T.,Imoto, T.
Analysis of the stabilization of hen lysozyme by helix macrodipole and charged side chain interaction.
J.Biochem.(Tokyo), 121:1076-1081, 1997

PubMed Abstract: In the N-terminal region of the alpha-helix of the c-type lysozymes, two Asx residues exist at the 18th and 27th positions. Hen lysozyme has Asp18/Asn27 (18D/27N), and we prepared three mutant lysozymes, Asn18/Asn27 (18N/27N), Asn18/Asp27 (18N/27D), and Asp18/Asp27 (18D/27D). The stability of the wild-type (18D/27N) lysozyme supported the existence of a hydrogen bond between the side chain of Asp18 and the amide group at the N1 position in the alpha-helix, while the stability of the 18N/27D lysozyme supported the presence of the capping box between the Ser24 (N-cap) and Asp27 residues. Although electrostatic repulsion was observed between Asp18 and Asp27 residues in 18D/27D lysozyme, the dissociation of each residue contributed to stabilizing the B-helix in 18D/27D lysozyme through hydrogen bonding and charge-helix macrodipole interaction. This is the first evidence that two neighboring negative charges at the N-terminus of the helix both increased the stability of the protein.

PubMed: 9354379

実験手法

X-RAY DIFFRACTION (1.79 Å)