NDLI: Structural and Thermodynamic Responses of Mutations at a Ca2+ Binding Site Engineered into Human Lysozyme

Content Provider	Journal of Biological Chemistry (JBC)
Author	Kuroki, Ryota Yutani, Katsuhide
Abstract	Structural determinants of Ca2+binding sites within proteins typically comprise several acidic residues in appropriate juxtaposition. Three residues (Ala-83, Gln-86, and Ala-92) in human lysozyme are characteristically mutated to Lys, Asp, and Asp, respectively, in natural Ca2+ binding lysozymes and α-lactalbumins. The effects of these mutations on the stability and Ca2+ binding properties of human lysozyme were investigated using calorimetry and were interpreted with crystal structures. The double mutant, in which Glu-86 and Ala-92 were replaced with Asp, clearly showed Ca2+ binding affinity, whereas neither point mutant showed Ca2+ affinity, indicating that both residues are essential. The further mutation of Ala-83 → Lys did not affect the Ca2+ binding of the double mutant. The point mutations Ala-83 → Lys and Glu-86 → Asp did not affect the stability, whereas the mutation Ala-92 → Asp was about 1.3 kcal/mol less stable. Structural analyses showed that both Asp-86 and Lys-83 were exposed to solvent. Side chains of Asp-86 and Asp-91 were rotated in opposite directions about χ1 angle, as if to reduce the electrostatic repulsion. The charged amino acids at the Ca2+ binding site did not significantly affect stability of the protein, possibly because of the local conformational change of the side chains.
Related Links	http://www.jbc.org/content/273/51/34310.abstract
Ending Page	34315
Starting Page	34310
Page Count	6
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	51
Volume Number	273
DOI	10.1074/jbc.273.51.34310
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	1998-12-18
Access Restriction	Open
Subject Keyword	PROTEIN CHEMISTRY AND STRUCTURE
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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