1KXX

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

Summary for 1KXX

• Entry DOI: 10.2210/pdb1kxx/pdb
• Descriptor: LYSOZYME (2 entities in total)
• Functional Keywords: hydrolase, glycosidase, electrostatic interaction, helix, hen lysozyme, stability
• Biological source: Gallus gallus (chicken)
• Cellular location: Secreted: P00698
• Total number of polymer chains: 1
• Total formula weight: 14331.16

Authors

Motoshima, H.,Ohmura, T.,Ueda, T.,Imoto, T. (deposition date: 1996-11-22, release date: 1997-11-26, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.71 Å)