1ssw
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(New page: 200px<br /><applet load="1ssw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ssw, resolution 2.13Å" /> '''Crystal structure of...)
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Revision as of 00:30, 21 November 2007
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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 with BME as ligand. Active as Lysozyme, with EC number 3.2.1.17 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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