X-Ray Crystallographic Analysis of Pokeweed Antiviral Protein-II after Reductive Methylation of Lysine Residues
| Autor: | I.V. Kurinov, C. Mao, Fatih M. Uckun, James D. Irvin |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Protein Conformation
Lysine Ribosome-inactivating protein Biophysics Chemical modification Cell Biology Methylation Ribosomal RNA Crystallography X-Ray Phosphate Biochemistry chemistry.chemical_compound Crystallography Protein structure chemistry Phytolacca americana Ribosome Inactivating Proteins Type 1 N-Glycosyl Hydrolases Molecular Biology Plant Proteins |
| Zdroj: | Biochemical and Biophysical Research Communications. 275:549-552 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.2000.3329 |
| Popis: | Pokeweed antiviral protein II (PAP-II) is a naturally occurring protein isolated from early summer leaves of the pokeweed plant (Phytolacca americana). PAP-II belongs to a family of ribosome-inactivating proteins which catalytically deadenylate ribosomal and viral RNA. The chemical modification of PAP-II by reductive methylation of its lysine residues significantly improved the crystal quality for X-ray diffraction studies. Hexagonal crystals of the modified PAP-II, with unit cell parameters a = b = 92.51 A, c = 79.05 A, were obtained using 1.8 M Na/K phosphate as the precipitant. These crystals contained one enzyme molecule per asymmetric unit and diffracted up to 2.4 A, when exposed to a synchroton source. |
| Databáze: | OpenAIRE |
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