Structure of a mutant Β toxin from Staphylococcus aureus reveals domain swapping and conformational flexibility

Andrew C. Kruse, Medora J. Huseby, Ke Shi, Jeff Digre, Douglas H. Ohlendorf, Cathleen A. Earhart

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)438-441
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume67
Issue number4
DOIs
StatePublished - Apr 1 2011

Keywords

  • Staphylococcus aureus
  • domain swapping
  • sphingomyelinase
  • Β toxin

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