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1: Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2159-61. Epub 2002 Nov 23.Click here to read Links

Cloning, expression, purification and preliminary X-ray crystallographic studies of 2-methylisocitrate lyase from Salmonella typhimurium.

Simanshu DK, Satheshkumar PS, Parthasarathy S, Savithri HS, Murthy MR.

Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India.

In Salmonella typhimurium, propionate is oxidized to pyruvate via the 2-methylcitric acid cycle. The last step of this cycle, the cleavage of 2-methylisocitrate to succinate and pyruvate, is catalysed by 2-methylisocitrate lyase (EC 4.1.3.30). Methylisocitrate lyase (molecular weight 32 kDa) with a C-terminal polyhistidine affinity tag has been cloned and overexpressed in Escherichia coli and purified and crystallized under different conditions using the hanging-drop vapour-diffusion technique. Crystals belong to the orthogonal space group P2(1)2(1)2(1), with unit-cell parameters a = 63.600, b = 100.670, c = 204.745 A. A complete data set to 2.5 A resolution has been collected using an image-plate detector system mounted on a rotating-anode X-ray generator.

PMID: 12454486 [PubMed - indexed for MEDLINE]