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Structure of the Month: S. aureus leucotoxin LukE

S. aureus protein structure
S. aureus leucotoxin structure, determined by the Center for Structural Genomics of Infectious Diseases.

 

Staphylococcus aureus is a type of bacteria that can cause skin infections, pneumonia, food poisoning, toxic shock syndrome, and blood poisoning. About one-third of people in the world have S. aureus bacteria on their bodies at any given time, primarily in the nose and on the skin. The bacteria can be present without causing an active infection.

Some strains of S. aureus produce specific factors that increase the spread, severity, and virulence of infection within the host. One such class of factors, the leukocidins, are pore-forming toxins consisting of two protein subunits. It is known that leukocidins have a destructive effect on human white blood cells, such as polymorphonuclear leucocytes, monocytes, and macrophages. To better understand how leukocidins may affect human immune cells, the Center for Structural Genomics of Infectious Diseases has determined the 3.2 Å resolution crystal structure of a subunit, leucotoxin LukE, from S. aureus subspecies aureus COL. The protein is predominantly beta-stranded (53%, 22 beta-strands) with 3% helical component, which defines the beta-barrel hetero-oligomeric architecture in transmembrane pore formation with its other subunit LukD.

For more information, please see the Protein Data Bank entry 3ROH.

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Last Updated June 06, 2011

Last Reviewed June 03, 2011