3k55 | pdb_00003k55

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Structure of beta hairpin deletion mutant of beta toxin from Staphylococcus aureus

spinqualitylabelsall models 3k55, resolution 3.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3k55 is a 16 chain structure with sequence from Staphylococcus aureus rn4220. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, NA Gene: hlb (Staphylococcus aureus RN4220) Activity: Sphingomyelin phosphodiesterase, with EC number 3.1.4.12 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Warning: this is a large structure, and loading might take a long time or not happen at all. Publication Abstract from PubMed The 3.35 A resolution crystal structure of a mutant form of the staphylococcal sphingomyelinase beta toxin in which a conserved hydrophobic beta-hairpin has been deleted is reported. It is shown that this mutation induces domain swapping of a C-terminal beta-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. Structure of a mutant beta toxin from Staphylococcus aureus reveals domain swapping and conformational flexibility.,Kruse AC, Huseby MJ, Shi K, Digre J, Ohlendorf DH, Earhart CA Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Apr 1;67(Pt, 4):438-41. Epub 2011 Mar 24. PMID:21505235 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Hemolysin

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