4IEN

Crystal Structure of Acyl-CoA Hydrolase from Neisseria meningitidis FAM18

Summary for 4IEN

• Entry DOI: 10.2210/pdb4ien/pdb
• Descriptor: Putative acyl-CoA hydrolase, COENZYME A, GUANOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• Functional Keywords: hot dog fold, hydrolase
• Biological source: Neisseria meningitidis
• Total number of polymer chains: 4
• Total formula weight: 78088.58

Authors

Khandokar, Y.B.,Forwood, J.K. (deposition date: 2012-12-13, release date: 2013-01-16, Last modification date: 2024-10-30)

Primary citation

Khandokar, Y.B.,Londhe, A.,Patil, S.,Forwood, J.K.
Expression, purification and crystallization of acetyl-CoA hydrolase from Neisseria meningitidis.
Acta Crystallogr.,Sect.F, 69:1303-1306, 2013

PubMed Abstract: 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 Å resolution at the Australian Synchrotron and belonged to space group P2(1)3 (unit-cell parameters a = b = c = 152.2 Å), with four molecules in the asymmetric unit.

PubMed: 24192375
DOI: 10.1107/S1744309113028042

Experimental method

X-RAY DIFFRACTION (2 Å)