posters 5th Asia-Pacific NMR Symposium 2013

A secreted haem binding protein from the oral pathogen Porphyromonas gingivalis (#127)

Daniel Collins 1 , Ann Kwan 2 , David Gell 1
  1. University of Tasmania, Hobart, TAS, Australia
  2. University of Sydney, Sydney, NSW, Australia

Porphyromonas gingivalis is a causative agent of chronic periodontitis, a disease involving progressive destruction of soft and hard tissues that support the teeth. P. gingivalis infection is also linked to increased atherosclerosis and rheumatoid arthritis. P. gingivalis lacks two enzymes in the porphyrin biosynthesis pathway and obtains porphyrins, together with the essential nutrient iron, by scavenging Fe-protoporphyrin-IX (haem) from the host. Haem uptake system component A (HusA) is a haem-binding protein that is essential for growth under conditions of low environmental haem (1). HusA is not homologous to any known haem-binding protein, suggesting that it adopts a new haem-binding fold. We are investigating the structure and porphyrin-binding function of HusA using NMR.

1.  Gao, J. L., Nguyen, K. A., and Hunter, N. (2010) Characterization of a hemophore-like protein from Porphyromonas gingivalis, J Biol Chem 285, 40028-40038.