1i22: Difference between revisions

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[[Image:1i22.gif|left|200px]]
{{Seed}}
[[Image:1i22.png|left|200px]]


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{{STRUCTURE_1i22|  PDB=1i22  |  SCENE=  }}  
{{STRUCTURE_1i22|  PDB=1i22  |  SCENE=  }}  


'''MUTANT HUMAN LYSOZYME (A83K/Q86D/A92D)'''
===MUTANT HUMAN LYSOZYME (A83K/Q86D/A92D)===




==Overview==
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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 --&gt; Lys did not affect the Ca2+ binding of the double mutant. The point mutations Ala-83 --&gt; Lys and Glu-86 --&gt; Asp did not affect the stability, whereas the mutation Ala-92 --&gt; 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.
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{{ABSTRACT_PUBMED_9852096}}


==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Mutant human lysozyme]]
[[Category: Mutant human lysozyme]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:28:53 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:17:49 2008''

Revision as of 07:17, 1 July 2008

File:1i22.png

Template:STRUCTURE 1i22

MUTANT HUMAN LYSOZYME (A83K/Q86D/A92D)

Template:ABSTRACT PUBMED 9852096

About this Structure

1I22 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

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