Literature summary extracted from
Yousef, M.S.; Bischoff, N.; Dyer, C.M.; Baase, W.A.; Matthews, B.W.
Guanidinium derivatives bind preferentially and trigger long-distance conformational changes in an engineered T4 lysozyme (2006), Protein Sci., 15, 853-861.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
3.2.1.17 |
the crystal structure of the switch mutant L20/R63A liganded to both methyl- and ethylguanidinium ions is determined at resolutions of 1.7 A and 1.8 A, respectively |
Tequatrovirus T4 |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
3.2.1.17 |
additional information |
L20 is a mutant with a molecular switch in a T4 lysozyme construct that promotes a large-scale (about 20 A) translocation of an alpha-helix but is unrelated to the function of the protein. The design is based in part on the use of a duplicated helical sequenc. When Arg63 is truncated to Ala (in mutant L20/R63A), the stability of the protein is reduced by 6.1°C relative to L20. In high salt buffer similar to that used for crystallization, the melting temperature of L20/R63A is increased by 2.2°C in the presence of either 200 mM methylguanidinium or 200 mM ethylguanidinium ion |
Tequatrovirus T4 |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
3.2.1.17 |
Tequatrovirus T4 |
P00720 |
- |
- |