Journal article

Identification of two dihydrodipicolinate synthase isoforms from Pseudomonas aeruginosa that differ in allosteric regulation

Rachael E Impey, Santosh Panjikar, Cody J Hall, Lucy J Bock, J Mark Sutton, Matthew A Perugini, Tatiana P Soares da Costa

The FEBS Journal | WILEY | Published : 2019


Pseudomonas aeruginosa is one of the leading causes of nosocomial infections, accounting for 10% of all hospital-acquired infections. Current antibiotics against P. aeruginosa are becoming increasingly ineffective due to the exponential rise in drug resistance. Thus, there is an urgent need to validate and characterise novel drug targets to guide the development of new classes of antibiotics against this pathogen. One such target is the diaminopimelate (DAP) pathway, which is responsible for the biosynthesis of bacterial cell wall and protein building blocks, namely meso-DAP and lysine. The rate limiting step of this pathway is catalysed by the enzyme dihydrodipicolinate synthase (DHDPS), ty..

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Awarded by National Health and Medical Research Council of Australia

Awarded by Australian Research Council

Funding Acknowledgements

We thank Prof Juliet Gerrard (The University of Auckland) for providing the dapA and dapB plasmids from E. coli. TPSC acknowledges the National Health and Medical Research Council of Australia (APP1091976) and Australian Research Council (DE190100806) for fellowship support, and MAP the Australian Research Council for funding support (DP150103313). REI is supported by an Australian Research Training scholarship and acknowledges the British Society for Antimicrobial Chemotherapy for funding support. We acknowledge the use of the MX2 beamline at the Australian Synchrotron and the CSIRO Collaborative Crystallisation Centre (www.csiro/C3; Melbourne, Australia). We also thank the La Trobe University Comprehensive Proteomics Platform for providing infrastructure support.