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)''' | + | {{Structure |
| + | |PDB= 1i20 |SIZE=350|CAPTION= <scene name='initialview01'>1i20</scene>, resolution 1.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Deoxyribodipyrimidine_endonucleosidase Deoxyribodipyrimidine endonucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.17 3.2.2.17] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''MUTANT HUMAN LYSOZYME (A92D)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1I20 is a [ | + | 1I20 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I20 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9852096 9852096] |
[[Category: Deoxyribodipyrimidine endonucleosidase]] | [[Category: Deoxyribodipyrimidine endonucleosidase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: mutant human lysozyme]] | [[Category: mutant human lysozyme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:44:28 2008'' |
Revision as of 09:44, 20 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Deoxyribodipyrimidine endonucleosidase, with EC number 3.2.2.17 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MUTANT HUMAN LYSOZYME (A92D)
Contents |
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.
Disease
Known diseases associated with this structure: Amyloidosis, renal OMIM:[153450], Microphthalmia, syndromic 1 OMIM:[309800]
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
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