1ix0
From Proteopedia
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|PDB= 1ix0 |SIZE=350|CAPTION= <scene name='initialview01'>1ix0</scene>, resolution 1.8Å | |PDB= 1ix0 |SIZE=350|CAPTION= <scene name='initialview01'>1ix0</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene> | + | |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] | + | |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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2bqa|2BQA]] | ||
| + | |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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==Overview== | ==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. | 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. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: Amyloidosis, renal OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=153450 153450]], Microphthalmia, syndromic 1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=309800 309800]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Yamagata, Y.]] | [[Category: Yamagata, Y.]] | ||
[[Category: Yutani, K.]] | [[Category: Yutani, K.]] | ||
| - | [[Category: NA]] | ||
[[Category: stability]] | [[Category: stability]] | ||
[[Category: water]] | [[Category: water]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:25:47 2008'' |
Revision as of 18:25, 30 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Related: | 2BQA
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 21:25:47 2008
Categories: Homo sapiens | Lysozyme | Single protein | Takano, K. | Yamagata, Y. | Yutani, K. | Stability | Water
