Journal article

Exploring the dihydrodipicolinate synthase tetramer: How resilient is the dimer-dimer interface?

Michael DW Griffin, Renwick CJ Dobson, Juliet A Gerrard, Matthew A Perugini

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | ELSEVIER SCIENCE INC | Published : 2010

Abstract

Dihydrodipicolinate synthase (DHDPS, E.C. 4.2.1.52) is a tetrameric enzyme that catalyses the first committed step of the lysine biosynthetic pathway. Dimeric variants of DHDPS have impaired catalytic activity due to aberrant protein motions within the dimer unit. Thus, it is thought that the tetrameric structure functions to restrict these motions and optimise enzyme dynamics for catalysis. Despite the importance of dimer-dimer association, the interface between subunits of each dimer is small, accounting for only 4.3% of the total monomer surface area, and the structure of the interface is not conserved across species. We have probed the tolerance of dimer-dimer association to mutation by ..

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Grants

Awarded by Royal Society of New Zealand Marsden


Awarded by Crop & Food Research Ltd


Awarded by Defense Threat Reduction Agency


Awarded by Australian Research Council


Funding Acknowledgements

This work was funded by the Royal Society of New Zealand Marsden Fund (Contract UOC303): Crop & Food Research Ltd, Contract C02X0001 for the New Economy Research Fund, Foundation for Research Science and Technology, New Zealand; Defense Threat Reduction Agency, Project AB07CBT004, and the Australian Research Council, Project DP0770888 and Australian Postdoctoral Fellowship (M.A.P.). R.C.J.D. holds a C.R. Roper Fellowship. M.D.W.G. holds a Melbourne Early Career Researcher Grant. We thank Jackie Healy for flagellating technical