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• W2040557064 abstract "The 3.35 Å resolution crystal structure of a mutant form of the staphylococcal sphingomyelinase β toxin in which a conserved hydrophobic β-hairpin has been deleted is reported. It is shown that this mutation induces domain swapping of a C-terminal β-strand, leading to the formation of dimers linked by a conformationally flexible hinge region. Eight dimers are seen in the asymmetric unit, exhibiting a broad spectrum of conformations trapped in place by intermolecular contacts within the crystal lattice. Furthermore, the 16 monomers within each asymmetric unit exhibit a remarkable heterogeneity in thermal factors, which can be accounted for by the varying degrees to which each monomer interacts with other molecules in the crystal. This structure provides a unique example of the challenges associated with crystallographic study of flexible proteins." @default.
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• W2040557064 date "2011-03-24" @default.
• W2040557064 modified "2023-09-27" @default.
• W2040557064 title "Structure of a mutant β toxin from<i>Staphylococcus aureus</i>reveals domain swapping and conformational flexibility" @default.
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• W2040557064 doi "https://doi.org/10.1107/s1744309111005239" @default.
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