Crystallization and Preliminary X-Ray Diffraction Analysis of PD-L4, a Ribosome Inactivating Protein from Phytolacca dioica L. leaves

Title: Crystallization and Preliminary X-Ray Diffraction Analysis of PD-L4, a Ribosome Inactivating Protein from Phytolacca dioica L. leaves

Volume: 14 Issue: 1

Author(s): Alessia Ruggiero, Angela Chambery, Antimo Di Maro, Marianna Pisante, Augusto Parente and Rita Berisio

Affiliation:

Keywords: Ribosome inactivating protein, Phytolacca dioica, crystallization, x-ray

Abstract: PD-L4, a type 1 ribosome inactivating protein from Phytolacca dioica leaves, has been successfully crystallized using vapour diffusion methods and PEG 4000 as a precipitant agent. In addition, crystals of a PD-L4 mutant, which has been recently observed to have a lower polynucleotide-adenosine glycosidase activity on DNA, rRNA and poly (A) substrates, have been obtained. To gather information on PD-L4 reaction mechanism both forms have been co-crystallized with adenine, the major product of their catalytic reaction. Diffraction patterns extend to atomic resolution and crystals belong to the orthorhombic P212121 space group, with one molecule in the asymmetric unit. Structure determination has been achieved using molecular replacement; preliminary electron density maps have clearly given evidence of adenine binding.

Cite this article as:

Ruggiero Alessia, Chambery Angela, Di Maro Antimo, Pisante Marianna, Parente Augusto and Berisio Rita, Crystallization and Preliminary X-Ray Diffraction Analysis of PD-L4, a Ribosome Inactivating Protein from Phytolacca dioica L. leaves, Protein & Peptide Letters 2007; 14 (1) . https://dx.doi.org/10.2174/092986607779117209

DOI https://dx.doi.org/10.2174/092986607779117209	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305