Structural basis of lipoprotein signal peptidase II action and inhibition by the antibiotic globomycin

Insight into a bacterial membrane protease Lipoproteins have key functions in many bacteria. They are synthesized in a precursor form that requires processing by enzymes that are essential in many pathogenic bacteria but have no equivalent in humans, making them potential drug targets. LspA is a key membrane protein involved in lipoprotein maturation in the bacterium Pseudomonas aeruginosa . Vogeley et al. determined the crystal structure of LspA bound to the antibiotic globomycin. Their structure and mutagenesis studies reveal how LspA processes substrate lipoproteins and indicate that globomycin inhibits the enzyme by binding to the active site. These findings should be useful in the development of new antibiotics. Science , this issue p. 876