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Publication Abstract from PubMed

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 290 K using ammonium phosphate as a precipitant. Optimized crystals diffracted to 2.0 A resolution at the Australian Synchrotron and belonged to space group P2(1)3 (unit-cell parameters a = b = c = 152.2 A), with four molecules in the asymmetric unit.

Expression, purification and crystallization of acetyl-CoA hydrolase from Neisseria meningitidis.,Khandokar YB, Londhe A, Patil S, Forwood JK Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Nov;69(Pt 11):1303-6. doi:, 10.1107/S1744309113028042. Epub 2013 Oct 30. PMID:24192375^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.