1ssw
From Proteopedia
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| - | [[Image:1ssw.gif|left|200px]] | + | [[Image:1ssw.gif|left|200px]] |
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| - | '''Crystal structure of phage T4 lysozyme mutant Y24A/Y25A/T26A/I27A/C54T/C97A''' | + | {{Structure |
| + | |PDB= 1ssw |SIZE=350|CAPTION= <scene name='initialview01'>1ssw</scene>, resolution 2.13Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</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= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of phage T4 lysozyme mutant Y24A/Y25A/T26A/I27A/C54T/C97A''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1SSW is a [ | + | 1SSW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SSW OCA]. |
==Reference== | ==Reference== | ||
| - | Alanine-scanning mutagenesis of the beta-sheet region of phage T4 lysozyme suggests that tertiary context has a dominant effect on beta-sheet formation., He MM, Wood ZA, Baase WA, Xiao H, Matthews BW, Protein Sci. 2004 Oct;13(10):2716-24. Epub 2004 Aug 31. PMID:[http:// | + | Alanine-scanning mutagenesis of the beta-sheet region of phage T4 lysozyme suggests that tertiary context has a dominant effect on beta-sheet formation., He MM, Wood ZA, Baase WA, Xiao H, Matthews BW, Protein Sci. 2004 Oct;13(10):2716-24. Epub 2004 Aug 31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15340171 15340171] |
[[Category: Bacteriophage t4]] | [[Category: Bacteriophage t4]] | ||
[[Category: Lysozyme]] | [[Category: Lysozyme]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''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 14:09:16 2008'' |
Revision as of 12:09, 20 March 2008
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| , resolution 2.13Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Lysozyme, with EC number 3.2.1.17 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of phage T4 lysozyme mutant Y24A/Y25A/T26A/I27A/C54T/C97A
Overview
In general, alpha-helical conformations in proteins depend in large part on the amino acid residues within the helix and their proximal interactions. For example, an alanine residue has a high propensity to adopt an alpha-helical conformation, whereas that of a glycine residue is low. The sequence preferences for beta-sheet formation are less obvious. To identify the factors that influence beta-sheet conformation, a series of scanning polyalanine mutations were made within the strands and associated turns of the beta-sheet region in T4 lysozyme. For each construct the stability of the folded protein was reduced substantially, consistent with removal of native packing interactions. However, the crystal structures showed that each of the mutants retained the beta-sheet conformation. These results suggest that the structure of the beta-sheet region of T4 lysozyme is maintained to a substantial extent by tertiary interactions with the surrounding parts of the protein. Such tertiary interactions may be important in determining the structures of beta-sheets in general.
About this Structure
1SSW is a Single protein structure of sequence from Bacteriophage t4. Full crystallographic information is available from OCA.
Reference
Alanine-scanning mutagenesis of the beta-sheet region of phage T4 lysozyme suggests that tertiary context has a dominant effect on beta-sheet formation., He MM, Wood ZA, Baase WA, Xiao H, Matthews BW, Protein Sci. 2004 Oct;13(10):2716-24. Epub 2004 Aug 31. PMID:15340171
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