Valentina Di Francesco
A team of researchers from the Seattle Structural Genomics Center for Infectious Disease (SSGCID), the Defence Science and Technology Laboratory (Dstl), United Kingdom (UK), and the University of Exeter, UK, have solved a three-dimensional protein structure of a macrophage infectivity potentiator (Mip), a novel virulence factor from the bacterium Burkholderia pseudomallei. B. pseudomallei causes the potentially fatal human disease melioidosis and is resistant to many antibiotics. Mips are peptidyl-prolyl cis-trans isomerases, enzymes required to catalyse protein folding. Inhibition of this enzyme activity may represent a novel antimicrobial approach to treat melioidosis.
Using nuclear magnetic resonance and X ray crystallography, researchers determined the structure of the protein, (BupsA.00130.a, PDB 2KE0), and it was found to bind to a small helical peptide, suggesting that Mips have roles in protein-protein interactions in addition to their enzyme activity. Furthermore, the protein was found to bind to the inhibitor cycloheximide-N-ethylethanoate which provides a basis for development of novel drug development.
Last Updated August 01, 2011
Last Reviewed August 01, 2011