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Structural and functional biology

  Antimicrobial targets

Bacterial Pathogenesis

Bioinformatics

Host pathogen interactions

Innate Immunity

Proteomics

Structural & functional biology

Vaccine development

Proteins are the molecular machines of all living organisms and the malfunctioning of proteins is a major cause of disease. Knowledge of the precise shape of a protein provides an understanding, at the atomic level, of how a protein functions. X-ray crystallography reveals fundamental insights into the structure of proteins and their mechanisms of action as well as providing a basis for the design of antimicrobial compounds.  
 
The ARC Centre of Excellence in Structural and Functional Microbial Genomics determines the 3D structure of proteins by X-ray crystallography at the Monash University Protein Crystallography Unit (PCU). The Centre also has priority access to the Australian Synchroton.
 
The Centre has a range of projects elucidating the structures, and/or their mechanism(s) of action, of the following proteins:
 
MACPF superfamily;
Membrane protein, TcpH, in Clostridium perfringes;
Major proteaeses involved in virulence in Dichelobacter nodosus;
CD1 glycoproteins
Lysins;
AB5 toxin in Escherichia coli;
Virulence-associated proteins in Legionella and;
Drug targets in Mycobacterium spp.;
 
For further information about the projects on MACPF, C. perfringens or D. nodosus proteins or lysins, please contact Centre Chief Investigator Professor James Whisstock.
 
For further information about the projects on CD1 glycoproteins, AB5 toxin, Legionella proteins or Mycobacterium spp. drug targets, please contact Centre Chief Investigator and Monash University Protein Crystallography Head, Professor Jamie Rossjohn.
 
Australian Research Council
Monash University
Victorian Government
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