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Structure of the Month: Burkholderia pseudomallei Mip

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.

B. pseudomallei Mip structure
B. pseudomallei Mip structure, determined by the Seattle Structural Genomics Center for Infectious Disease (SSGCID), the Defence Science and Technology Laboratory (Dstl), UK, and the University of Exeter.

 

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.


Reference

Norville I, O’Shea K, Sarkar-Tyson M, Zheng S, Titball RW, Varani G, Harmer NJ. 2011 The structure of a Burkholderia pseudomallei immunophilin-inhibitor complex reveals new approaches to antimicrobial development. Biochem J. May 16. PMID: 21574961

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Last Updated August 01, 2011

Last Reviewed August 01, 2011