Jodie Johnston

LecturerJodie Johnston

West 848
Internal Phone: 93044

Qualifications & Memberships

Research Interests

My research interests are related to studying the structure and function of proteins, the aim being to obtain a better understanding of key biological questions at level of atoms and molecules.

My research interests encompass the following areas:

-Understanding proteins from microbial pathogens, especially those involved in essential metabolic pathways or otherwise important for pathogenicity, bacterial survival and anti-microbial resistance (e.g. proteins from the TB-causing bacteria M.tuberculosis (M.tb) and the opportunistic pathogen S. aureus).

The aim being to understand not only the role of these proteins in the bacteria and disease, but also uses structural information to design inhibitors that could become future drugs to treat microbial

-Understanding the molecular basis and communication networks behind protein cooperativty and allostery

-Bio-engineering proteins to act as tools in a range of applications

Recent Publications

  • Gerth ML., Liu Y., Jiao W., Zhang XX., Baker EN., Lott JS., Rainey PB. and Johnston JM. (2017) Crystal structure of a bicupin protein HutD involved in histidine utilization in Pseudomonas. Proteins: Structure, Function and Bioinformatics 85(8): 1580-1588.
  • Jirgis ENM., Bashiri G., Bulloch EMM., Johnston JM. and Baker EN. (2016) Structural Views along the Mycobacterium tuberculosis MenD Reaction Pathway Illuminate Key Aspects of Thiamin Diphosphate-Dependent Enzyme Mechanisms. Structure 24(7): 1167-1177.
  • Jung J., Bashiri G., Johnston JM. and Baker EN. (2016) Mass spectral determination of phosphopantetheinylation specificity for carrier proteins in Mycobacterium tuberculosis. FEBS Open Bio 6(12): 1220-1226.
  • Bashiri G., Johnston JM., Evans GL., Bulloch EMM., Goldstone DC., Jirgis ENM., Kleinboelting S., Castell A., Ramsay RJ. and Manos-Turvey A. (2015) Structure and inhibition of subunit I of the anthranilate synthase complex of Mycobacterium tuberculosis and expression of the active complex. Acta Crystallographica Section D Biological Crystallography 71(11): 2297-2308.
  • Chai A-F., Bulloch EMM., Evans GL., Lott JS., Baker EN. and Johnston JM. (2015) A covalent adduct of MbtN, an acyl-ACP dehydrogenase from Mycobacterium tuberculosis , reveals an unusual acyl-binding pocket. Acta Crystallographica Section D Biological Crystallography 71(4): 862-872.