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Structure of a mutant β toxin from Staphylococcus aureus reveals domain swapping and conformational flexibility
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...
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| Main Authors: | , , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado: |
International Union of Crystallography
2011
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| Assuntos: | |
| Acceso en liña: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3080144/ https://ncbi.nlm.nih.gov/pubmed/21505235 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S1744309111005239 |
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