Monday 15 July 2013 4:28pm
SJWRI Molecular Microbiology PhD student Madhu Shankar, jointly supervised by Dr Brian Monk of the SJWRI and Dr Joel Tyndall of the National School of Pharmacy, has published the crystal structure of the enzyme lumazine synthase from the fungal pathogen Candida glabrata in the highly regarded biological crystallography journal Acta Crystallographa D, which has an Impact Factor of 14.1.
Candida glabrata has emerged as an important fungal pathogen with intrinsic resistance to azole drugs, and this is driving the need to identify new drug targets. Lumazine synthase is part of the riboflavin-biosynthesis pathway, which is essential to fungi and bacteria and is a potential drug target for the development of broad-spectrum antifungal drugs.
The X-ray crystal structure of recombinant lumazine synthase from C. glabrata was obtained at 2.24 Angstrom resolution, and revealed a dimer of homopentamers, with one in five subunits containing a product molecule from the catalytic reaction.
This is the first crystal structure of a protein published by researchers working in the SJWRI.
X-ray crystal structure of recombinant enzyme lumazine synthase from C. glabrata, complexed with the product of catalysis. Image via Madhu Shankar, PhD student.