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Structure of the Month: EpiD Protein Structure

Bacteria produce a wide range of antimicrobial peptides, or small proteins that kill or slow the growth of other microbes. These peptides protect bacteria from competing microbes. For example, the Staphylococcus bacteria species produce and secrete a compound known as epidermin. Antimicrobial peptides such as epidermin exhibit highly potent biological activities, ranging from antimicrobial activity against methicillin-resistant Staphylococcus aureus (MRSA) to anticancer activity against mouse leukemia cells. These compounds may facilitate novel therapeutic approaches or drug development for antimicrobial resistant pathogens.

The maturation of epidermin requires a series of modification reactions to change its chemical structure. EpiD protein, whose three-dimensional structure is shown here, catalyzes the first modification of epidermin, the decarboxylation of the C-terminal cysteine residue. EpiD is essential for epidermin biosynthesis.

Information about structure of epidermin-biosynthesis protein EpiD can be found at the Center for Structural Genomics of Infectious Diseases (CSGID) webpage, and the Protein Data Bank entry 3QJG.

EpiD protein structure
Biological assembly of EpiD protein consists of 12 monomers grouped in 4 trimers to form a sphere. The picture shows 3 protein trimers in front and the forth, shown as semi-transparent, in the background. The structure contains flavin mononucleotide (FMN), shown in black, which is necessary for EpiD biological activity.

 

Past Features

Last Updated April 01, 2011

Last Reviewed April 01, 2011