Journal article
Substrate Locking Promotes Dimer-Dimer Docking of an Enzyme Antibiotic Target
SC Atkinson, C Dogovski, K Wood, MDW Griffin, MA Gorman, L Hor, CF Reboul, AM Buckle, J Wuttke, MW Parker, RCJ Dobson, MA Perugini
Structure | CELL PRESS | Published : 2018
Abstract
Atkinson et al. show that pyruvate binding locks the conformation of the C. botulinum DHDPS dimer that promotes tetramerization. They describe a new method (ProD-MS) that assesses protein dynamics on a slow (second-minute) timescale.
Grants
Awarded by Army Research Laboratory
Funding Acknowledgements
We acknowledge the support and assistance of the friendly staff at the CSIRO Collaborative Crystallisation Centre; Australian Synchrotron; and La Trobe University-Comprehensive Proteomics Platform. We acknowledge the Australian Research Council for project funding (DP150103313) and Future Fellowships to M.A.P. (FT0991245) and M.D.W.G. (FT140100544); infrastructure support from the Australian Cancer Research Foundation and the Victorian Government Operational Infrastructure Support Scheme to St. Vincent's Institute; the National Health and Medical Research Council for fellowship support for S.C.A. (1072267) and M.W.P. (1021645). Travel to perform experiments at FRM-II was funded by the access to major facilities program, supported by the Commonwealth of Australia under the International Science Linkages program. R.C.J.D. acknowledges the following for funding support, in part: (1) the New Zealand Royal Society Marsden Fund (contract UOC1506); (2) the US Army Research Laboratory and US Army Research Office under contract/grant number W911NF-11-1-0481; and (3) the Biomolecular Interactions Centre (UC).