Crystal and molecular structure of RmlA Crystal and molecular structure of RmlA


Image and article by Dr. Magnus S. Alphey, University of St. Andrews

The crystals of RmlA are grown from recombinant RmlA protein. The protein is overexpressed in lab strains of E. coli cultured in Formedium LB broth supplemented with antibiotics. The recombinant RmlA protein is purified away from the cocktail of endogenous E. coli proteins using column chromatography.

RmlA (full name: glucose-1-phosphate thymidylyltransferase) is an enzyme involved in the L-rhamnose biosynthetic pathway of many microorganisms, including Mycobacterium tuberculosis and Pseudomonas aeruginosa. L-rhamnose is an important component of the cell wall. Understanding the molecular structure and function of RmlA helps to identify potential drugs that could weaken the bacterial cells and assist in the fight against infection.

Magnus S. Alphey, Lisa Pirrie, Leah S. Torrie, Wassila Abdelli Boulkeroua, Mary Gardiner, Aurijit Sarkar, Marko Maringer, Wulf Oehlmann, Ruth Brenk, Michael S. Scherman, Michael McNeil, Martin Rejzek, Robert A. Field, Mahavir Singh, David Gray, Nicholas J. Westwood, James H. Naismith (2013). Allosteric Competitive Inhibitors of the Glucose-1-Phosphate Thymidylyltransferase (RmlA) from Pseudomonas aeruginosa. ACS Chem. Biol. 8, pages 387-396.