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Literature summary for 3.2.1.17 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.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants Comment Organism
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

Organism UniProt Comment Textmining
Tequatrovirus T4 P00720
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