Prof David Leys PhD

Professor of Structural Biology

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Research interests

Macromolecular structure and function

We use x-ray crystallography to address how macromolecular structure determines function. We focus on several aspects: how do proteins interact with other macromolecules (RNA, DNA, proteins) or their substrates?  How do enzymes work, particularly those for which mechanistic insight is lacking? Protein structures also form the basis of protein engineering and for structure-based drug design. We are studying proteins of biotechnological interest (ie biofuel production) to provide for the much needed structural insight into these enzymes.


Mechanistic enzymology at the atomic level           Detailed insights into transcriptional regulation


Hot of the press: new paper in Nature on a PAS enzyme

Recent publications:

1. Karl A.P. Payne, Mark D. White, Karl Fisher, Basile Khara, Samuel S. Bailey, David Parker, Nicholas J.W. Rattray, Drupad K. Trivedi, Royston Goodacre, Rebecca Beveridge, Perdita Barran, Stephen E.J. Rigby, Nigel S. Scrutton, Sam Hay, David Leys (2015) New cofactor supports reversible decarboxylation of α,β-unsaturated acids via 1,3-dipolar cycloaddition chemistry. Nature 522, 497–501
2. Mark D. White, Karl A.P. Payne, Karl Fisher, Stephen A. Marshall, David Parker, Nicholas J.W. Rattray, Drupad K. Trivedi, Royston Goodacre, Stephen E.J. Rigby, Nigel S. Scrutton, Sam Hay, David Leys (2015) UbiX is a flavin prenyltransferase required for bacterial ubiquinone biosynthesis. Nature 522, 502–507
3. Karl A.P. Payne, Carolina P. Quezada, Karl Fisher, Mark S. Dunstan, Fraser A. Collins, Hanno Sjuts, Colin Levy, Sam Hay, Stephen E.J. Rigby, David Leys (2015) Reductive dehalogenase structure suggest a mechanism for B12-dependent dehalogenation. Nature 517, 513-516
Mary Ortmayer, Pierre Lafite, Binuraj RK Menon, Tewes Tralau, Karl Fisher, Lukas Denkhaus, Nigel S Scrutton, Stephen EJ Rigby, Andrew W Munro, Sam Hay, David Leys (2016) An oxidative N-demethyase reveals PAS transition from ubiquitous sensor to enzyme. Nature doi:10.1038/nature20159



Research and projects