1l18
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
- | |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= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l18 OCA], [http://www.ebi.ac.uk/pdbsum/1l18 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l18 RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
- | 1L18 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1L18 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L18 OCA]. |
==Reference== | ==Reference== | ||
Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3., Matsumura M, Becktel WJ, Matthews BW, Nature. 1988 Aug 4;334(6181):406-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/3405287 3405287] | Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3., Matsumura M, Becktel WJ, Matthews BW, Nature. 1988 Aug 4;334(6181):406-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/3405287 3405287] | ||
- | [[Category: | + | [[Category: Enterobacteria phage t4]] |
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hydrolase (o-glycosyl)]] | [[Category: hydrolase (o-glycosyl)]] | ||
- | ''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 21:56:32 2008'' |
Revision as of 18:56, 30 March 2008
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, resolution 1.7Å | |||||||
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Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
HYDROPHOBIC STABILIZATION IN T4 LYSOZYME DETERMINED DIRECTLY BY MULTIPLE SUBSTITUTIONS OF ILE 3
Overview
Replacing the isoleucine at amino-acid position three of bacteriophage T4 lysozyme causes changes in the thermodynamic stability of the protein that are directly related to the hydrophobicity of the substituted residue. Structural analysis confirms that the hydrophobic stabilization is proportional to the reduction of the surface area accessible to solvent on folding.
About this Structure
1L18 is a Single protein structure of sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.
Reference
Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3., Matsumura M, Becktel WJ, Matthews BW, Nature. 1988 Aug 4;334(6181):406-10. PMID:3405287
Page seeded by OCA on Sun Mar 30 21:56:32 2008