Neisseria meningitidis is the causative microorganism of many human diseases, including bacterial meningitis; together with Streptococcus pneumoniae, it accounts for approximately 80% of bacterial meningitis infections. The emergence of antibiotic-resistant strains of N. meningitidis has created a strong urgency for the development of new therapeutics, and the high-resolution structural elucidation of enzymes involved in cell metabolism represents a platform for drug development. Acetyl-CoA hydrolase is involved in multiple functions in the bacterial cell, including membrane synthesis, fatty-acid and lipid metabolism, gene regulation and signal transduction. Here, the first recombinant protein expression, purification and crystallization of a hexameric acetyl-CoA hydrolase from N. meningitidis are reported. This protein was crystallized using the hanging-drop vapour-diffusion technique at pH 8.5 and 290K using ammonium phosphate as a precipitant. Optimized crystals diffracted to 2.0Ã… resolution at the Australian Synchrotron and belonged to space group P213 (unit-cell parameters a = b = c = 152.2Ã…), with four molecules in the asymmetric unit.
|Number of pages||4|
|Journal||Acta Crystallographica Section F:Structural Biology Communications|
|Publication status||Published - Nov 2013|
Khandokar, Y., Londhe, A., Patil, S., & Forwood, J. (2013). Expression, purification and crystallization of acetyl-CoA hydrolase from Neisseria meningitides. Acta Crystallographica Section F:Structural Biology Communications, 69(11), 1303-1306. https://doi.org/10.1107/S1744309113028042