1ix0

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[[Image:1ix0.jpg|left|200px]]
[[Image:1ix0.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1ix0 |SIZE=350|CAPTION= <scene name='initialview01'>1ix0</scene>, resolution 1.8&Aring;
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The line below this paragraph, containing "STRUCTURE_1ix0", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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|GENE=
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{{STRUCTURE_1ix0| PDB=1ix0 | SCENE= }}
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|RELATEDENTRY=[[2bqa|2BQA]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ix0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ix0 OCA], [http://www.ebi.ac.uk/pdbsum/1ix0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ix0 RCSB]</span>
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'''I59A-3SS human lysozyme'''
'''I59A-3SS human lysozyme'''
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[[Category: Yamagata, Y.]]
[[Category: Yamagata, Y.]]
[[Category: Yutani, K.]]
[[Category: Yutani, K.]]
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[[Category: stability]]
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[[Category: Stability]]
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[[Category: water]]
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[[Category: Water]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:31:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:25:47 2008''
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Revision as of 17:31, 2 May 2008

Template:STRUCTURE 1ix0

I59A-3SS human lysozyme


Overview

This study sought to attain a better understanding of the contribution of buried water molecules to protein stability. The 3SS human lysozyme lacks one disulfide bond between Cys77 and Cys95 and is significantly destabilized compared with the wild-type human lysozyme (4SS). We examined the structure and stability of the I59A-3SS mutant human lysozyme, in which a cavity is created at the mutation site. The crystal structure of I59A-3SS indicated that there were ordered new water molecules in the cavity created. The stability of I59A-3SS is 5.5 kJ/mol less than that of 3SS. The decreased stability of I59A-3SS (5.5 kJ/mol) is similar to that of Ile to Ala mutants with newly introduced water molecules in other globular proteins (6.3 +/- 2.1 kJ/mol), but is less than that of Ile/Leu to Ala mutants with empty cavities (13.7 +/- 3.1 kJ/mol). This indicates that water molecules partially compensate for the destabilization by decreasing hydrophobic and van der Waals interactions. These results provide further evidence that buried water molecules contribute to protein stability.

About this Structure

1IX0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Buried water molecules contribute to the conformational stability of a protein., Takano K, Yamagata Y, Yutani K, Protein Eng. 2003 Jan;16(1):5-9. PMID:12646687 Page seeded by OCA on Fri May 2 20:31:43 2008

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