3K55
Structure of beta hairpin deletion mutant of beta toxin from Staphylococcus aureus
Summary for 3K55
| Entry DOI | 10.2210/pdb3k55/pdb |
| Descriptor | Beta-hemolysin, CHLORIDE ION, SODIUM ION (3 entities in total) |
| Functional Keywords | beta toxin, hemolysin, sphingomyelinase, domain swapping, hydrolase |
| Biological source | Staphylococcus aureus |
| Total number of polymer chains | 16 |
| Total formula weight | 556124.79 |
| Authors | Kruse, A.C.,Huseby, M.,Shi, K.,Digre, J.,Ohlendorf, D.H.,Earhart, C.A. (deposition date: 2009-10-06, release date: 2011-01-26, Last modification date: 2024-11-20) |
| Primary citation | Kruse, A.C.,Huseby, M.J.,Shi, K.,Digre, J.,Ohlendorf, D.H.,Earhart, C.A. Structure of a mutant beta toxin from Staphylococcus aureus reveals domain swapping and conformational flexibility Acta Crystallogr.,Sect.F, 67:438-441, 2011 Cited by PubMed 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. PubMed: 21505235DOI: 10.1107/S1744309111005239 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.35 Å) |
Structure validation
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