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1i20
From Proteopedia
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[[Image:1i20.gif|left|200px]] | [[Image:1i20.gif|left|200px]] | ||
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'''MUTANT HUMAN LYSOZYME (A92D)''' | '''MUTANT HUMAN LYSOZYME (A92D)''' | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Kuroki, R.]] | [[Category: Kuroki, R.]] | ||
| - | [[Category: | + | [[Category: Calcium binding site]] |
| - | [[Category: | + | [[Category: Hydrolase]] |
| - | [[Category: | + | [[Category: Mutant human lysozyme]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:28:48 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 16:28, 2 May 2008
MUTANT HUMAN LYSOZYME (A92D)
Overview
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 alpha-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 chi1 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.
About this Structure
1I20 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural and thermodynamic responses of mutations at a Ca2+ binding site engineered into human lysozyme., Kuroki R, Yutani K, J Biol Chem. 1998 Dec 18;273(51):34310-5. PMID:9852096 Page seeded by OCA on Fri May 2 19:28:48 2008
