Crystallization and preliminary X-ray diffraction analysis of PD-L4, a ribosome inactivating protein from Phytolacca dioica L. leaves.
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 P2(1)2(1)2(1) 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.
Ruggiero
Alessia
A
Istituto di Biostrutture e Bioimmagini, C.N.R., I-80134 Napoli, Italy.
Chambery
Angela
A
Di Maro
Antimo
A
Pisante
Marianna
M
Parente
Augusto
A
Berisio
Rita
R
D003460:Crystallization; D029603:Phytolacca / Q000737:chemistry*; D018515:Plant Leaves / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D054789:Ribosome Inactivating Proteins, Type 1 / Q000737:chemistry* / Q000302:isolation & purification; D012270:Ribosomes / Q000378:metabolism*; D014961:X-Ray Diffraction
D010940:Plant Proteins; D054789:Ribosome Inactivating Proteins, Type 1; C105087:PD-S2 protein, Phytolacca dioica