Destabilization of the Homotetrameric Assembly of 3-Deoxy-D-Arabino-Heptulosonate-7-Phosphate Synthase from the Hyperthermophile Pyrococcus furiosus Enhances Enzymatic Activity
Ali Reza Nazmi, Linley R Schofield, Renwick CJ Dobson, Geoffrey B Jameson, Emily J Parker
Journal of Molecular Biology | ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD | Published : 2014
Many proteins adopt homomeric quaternary structures to support their biological function, including the first enzyme of the shikimate pathway that is ultimately responsible for the biosynthesis of the aromatic amino acids in plants and microorganisms. This enzyme, 3-deoxy-d-arabino-heptulosonate-7-phosphate synthase (DAH7PS), adopts a variety of different quaternary structures depending on the organism in which it is found. The DAH7PS from the hyperthermophilic archaebacterium Pyrococcus furiosus was previously shown to be tetrameric in its crystalline form, and this quaternary association is confirmed in an improved structure in a different crystal system. This tetramer is also present in s..View full abstract
We are grateful to the suggestion made by a referee that the buried water associated with the buried Asp181 residues may well be protonated in the interests of charge neutrality. Part of this research was undertaken on the MX1, MX2 and SAXS/WAXS beamlines at the Australian Synchrotron, Victoria, Australia. We acknowledge support for these studies from the New Zealand Synchrotron Group and the Australian Synchrotron.