Simanshu , DK and Satheshkumar , PS and Parthasarathy , S and Savithri , HS and Murthy , MR (2002) Cloning, expression, purification and preliminary X-ray crystallographic studies of 2-methylisocitrate lyase from Salmonella typhimurium. Acta Crystallogr. In: Acta Crystallographica Section D Biological Crystallography, 58 (12). pp. 2159-2161.
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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 188.8.131.52). 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 Angstrom. A complete data set to 2.5 Angstrom resolution has been collected using an image-plate detector system mounted on a rotating-anode X-ray generator.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to International Union of Crystallography .|
|Keywords:||propionate catabolism; 2-methylisocitrate lyase.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||14 Dec 2010 06:30|
|Last Modified:||14 Dec 2010 06:30|
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