1c45: Difference between revisions
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[[Image:1c45.gif|left|200px]] | [[Image:1c45.gif|left|200px]] | ||
'''MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES''' | {{Structure | ||
|PDB= 1c45 |SIZE=350|CAPTION= <scene name='initialview01'>1c45</scene>, resolution 1.8Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] | |||
|GENE= | |||
}} | |||
'''MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1C45 is a [ | 1C45 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=1C45 OCA]. | ||
==Reference== | ==Reference== | ||
Effect of foreign N-terminal residues on the conformational stability of human lysozyme., Takano K, Tsuchimori K, Yamagata Y, Yutani K, Eur J Biochem. 1999 Dec;266(2):675-82. PMID:[http:// | Effect of foreign N-terminal residues on the conformational stability of human lysozyme., Takano K, Tsuchimori K, Yamagata Y, Yutani K, Eur J Biochem. 1999 Dec;266(2):675-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10561612 10561612] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
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[[Category: stability]] | [[Category: stability]] | ||
''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 10:19:35 2008'' | ||
Revision as of 11:19, 20 March 2008
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| , resolution 1.8Å | |||||||
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| Ligands: | |||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MUTANT HUMAN LYSOZYME WITH FOREIGN N-TERMINAL RESIDUES
OverviewOverview
To minutely understand the effect of foreign N-terminal residues on the conformational stability of human lysozyme, five mutant proteins were constructed: two had Met or Ala in place of the N-terminal Lys residue (K1M and K1A, respectively), and others had one additional residue, Met, Gly or Pro, to the N-terminal Lys residue (Met(-1), Gly(-1) and Pro(-1), respectively). The thermodynamic parameters for denaturation of these mutant proteins were examined by differential scanning calorimetry and were compared with that of the wild-type protein. Three mutants with the extra residue were significantly destabilized: the changes in unfolding Gibbs energy (DeltaDeltaG) were -9.1 to -12.2 kJ.mol-1. However, the stability of two single substitutions at the N-terminal slightly decreased; the DeltaDeltaG values were only -0.5 to -2.5 kJ.mol-1. The results indicate that human lysozyme is destabilized by an expanded N-terminal residue. The crystal structural analyses of K1M, K1A and Gly(-1) revealed that the introduction of a residue at the N-terminal of human lysozyme caused the destruction of hydrogen bond networks with ordered water molecules, resulting in the destabilization of the protein.
DiseaseDisease
Known diseases associated with this structure: Amyloidosis, renal OMIM:[153450], Microphthalmia, syndromic 1 OMIM:[309800]
About this StructureAbout this Structure
1C45 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Effect of foreign N-terminal residues on the conformational stability of human lysozyme., Takano K, Tsuchimori K, Yamagata Y, Yutani K, Eur J Biochem. 1999 Dec;266(2):675-82. PMID:10561612
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