个人简介

Tony Wilkinson trained for his PhD with Alan Fersht at Imperial College London working in protein engineering on tyrosyl tRNA synthetase. He joined the laboratory of James Wang at Harvard University working on DNA toposisomerases, and subsequently the lab of Guy Dodson at the University of York, learning protein crystallography working on ligand discrimination in oxygen transport proteins. He subsequently took up an academic post in the York Structural Biology Laboratory in the Chemistry Department where he is now a Professor. His group has studied sequence-independent peptide binding in transporter systems and transcriptional regulators in Bacillus with a focus on the control and execution of the process of cell development leading to the formation of dormant spores. More recently he has been working on proteins from the pathogens Plasmodium falciparum that causes malaria and Rhodococcus equi that causes lung disease in young horses.

研究领域

Structure and function of proteins involved in regulation

Professor Wilkinson’s group uses structural biology as a key tool to dissect structure and mechanism in proteins. On the one hand, we study systems of proteins that determine cellular fate during spore formation in Bacillus subtilis. On the other hand, we have specific interests in proteins that contribute to virulence in pathogens in humans and in livestock. Current projects include: Structural studies of the virulence-associated proteins of the horse pathogen Rhodococcus equi N-myristoyltranferase as a target for drug development to treat malaria and leishmaniasis Structural studies proteins involved in (i) cell fate determination, (ii) regulation of DNA replication and (iii) cellular engulfment during sporulation in Bacillus subtilis.

近期论文

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Discovery of Novel and Ligand-Efficient Inhibitors of Plasmodium falciparum and Plasmodium vivax N-Myristoyltransferase M D Rackham et al., J. Med. Chem., 2013, 56 (1), 371–375. Structure of Components of an Intercellular Channel Complex in Sporulating Bacillus subtilis. V M Levdikov et al., Proc. Natl. Acad. Sci. USA, 2012, 109, 5441-5445. Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis. P Nicolas et al., Science, 2012, 335, 1103-1106. Global Network Reorganization During Dynamic Adaptations of Bacillus subtilis Metabolism Buescher et al., Science, 2012, 335, 1099-1103 Structure of the Phosphatase Domain of the Cell Fate Determinant SpoIIE from Bacillus subtilis. V M Levdikov et al., J. Mol. Biol., 2012, 415, 343-358. Compensating stereochemical changes allow murein tripeptide to be accommodated in a conventional peptide binding protein. A Maqbool et al., J. Biol. Chem., 2011, 286, 31512-31521. N-myristoyltransferase from Leishmania donovani: Structural and Functional Characterisation of a Potential Drug Target for Visceral Leishmaniasis. J A Brannigan et al., J. Mol. Biol., 2010, 396, 985-999. N-myristoyltransferase inhibitors as new leads to treat sleeping sickness. J A Frearson et al., Nature, 2010, 464, 728-732.