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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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Wedi'i Gadw mewn:
Manylion Llyfryddiaeth
Prif Awduron: Kruse, Andrew C., Huseby, Medora J., Shi, Ke, Digre, Jeff, Ohlendorf, Douglas H., Earhart, Cathleen A.
Fformat: Artigo
Iaith:Inglês
Cyhoeddwyd: International Union of Crystallography 2011
Pynciau:
Mynediad Ar-lein: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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