The 2.5 A structure of pokeweed antiviral protein
| Autor: | Stephen R. Ernst, James D. Irvin, Arthur F. Monzingo, Edward J. Collins, Jon D. Robertus |
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| Rok vydání: | 1993 |
| Předmět: |
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Molecular Stereochemistry Molecular Sequence Data Substrate analog Ricin Crystallography X-Ray chemistry.chemical_compound Structural Biology Phytolacca americana Amino Acid Sequence Molecular Biology Peptide sequence N-Glycosyl Hydrolases Plant Proteins biology Pokeweed mitogen Active site Hydrogen Bonding Ribosomal RNA Ribonucleotides biology.organism_classification Phytolaccaceae chemistry Biochemistry biology.protein Mutagenesis Site-Directed Ribosome Inactivating Proteins Type 1 Formycins |
| Zdroj: | Journal of molecular biology. 233(4) |
| ISSN: | 0022-2836 |
| Popis: | The pokeweed antiviral protein (PAP), isolated from the leaves of Phytolacca americana, is one of a family of plant and bacterial ribosome-inhibiting proteins (RIPs) which act as specific N-glycosidases on rRNA. Here we report the three-dimensional structure of PAP determined to 2.5 A resolution by X-ray crystallography. After 14 rounds of refinement, the R factor is 0.17 for 5.0 to 2.5 A data. The protein is homologous with the A chain of ricin and exhibits a very similar folding pattern. The positions of key active site residues are also similar. We also report the 2.8 A structure of PAP complexed with a substrate analog, formycin 5'-monophosphate. As seen previously in ricin, the formycin ring is stacked between invariant tyrosines 72 and 123. Arg179 bonds to N-3 which is thought to be important in catalysis. |
| Databáze: | OpenAIRE |
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