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Título: | Overexpression, purification, crystallization and preliminary structural studies of p-coumaric acid decarboxylase from Lactobacillus plantarum |
Autor: | Rodríguez, Héctor CSIC ORCID; Rivas, Blanca de las CSIC ORCID; Muñoz, Rosario CSIC ORCID ; Mancheño, Jose M. CSIC ORCID | Palabras clave: | p-coumaric acid decarboxylase Lactobacillus plantarum |
Fecha de publicación: | 2007 | Editor: | John Wiley & Sons | Citación: | Acta Crystallographica Section F Structural Biology and Crystallization Communications 63: 300–303 (2007) | Resumen: | The substrate-inducible p-coumaric acid decarboxylase (PDC) from Lactobacillus plantarum has been overexpressed in Escherichia coli, purified and confirmed to possess decarboxylase activity. The recombinant His6-tagged enzyme was crystallized using the hanging-drop vapour-diffusion method from a solution containing 20%(w/v) PEG 4000, 12%(w/v) 2-propanol, 0.2 M sodium acetate, 0.1 M Tris–HCl pH 8.0 with 0.1 M barium chloride as an additive. Diffraction data were collected in-house to 2.04 A ° resolution. Crystals belonged to the tetragonal space group P43, with unit-cell parameters a = b = 43.15, c = 231.86 A ° . The estimated Matthews coefficient was 2.36 A ° 3 Da 1, corresponding to 48% solvent content, which is consistent with the presence of two protein molecules in the asymmetric unit. The structure of PDC has been determined by the molecular-replacement method. Currently, the structure of PDC complexed with substrate analogues is in progress, with the aim of elucidating the structural basis of the catalytic mechanism | Versión del editor: | http://dx.doi.org/10.1107/S1744309107008846 | URI: | http://hdl.handle.net/10261/45449 | DOI: | 10.1107/S1744309107008846 | ISSN: | 1744-3091 |
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