Ontology highlight
ABSTRACT:
SUBMITTER: Huseby M
PROVIDER: S-EPMC2168928 | biostudies-literature | 2007 Dec
REPOSITORIES: biostudies-literature
Huseby Medora M Shi Ke K Brown C Kent CK Digre Jeff J Mengistu Fikre F Seo Keun Seok KS Bohach Gregory A GA Schlievert Patrick M PM Ohlendorf Douglas H DH Earhart Cathleen A CA
Journal of bacteriology 20070914 23
Beta toxin is a neutral sphingomyelinase secreted by certain strains of Staphylococcus aureus. This virulence factor lyses erythrocytes in order to evade the host immune system as well as scavenge nutrients. The structure of beta toxin was determined at 2.4-A resolution using crystals that were merohedrally twinned. This structure is similar to that of the sphingomyelinases of Listeria ivanovii and Bacillus cereus. Beta toxin belongs to the DNase I folding superfamily; in addition to sphingomyel ...[more]