9X2O
X-ray structure of antiviral protein from Mirabilis jalapa
Summary for 9X2O
| Entry DOI | 10.2210/pdb9x2o/pdb |
| Descriptor | Antiviral protein MAP, SULFATE ION (3 entities in total) |
| Functional Keywords | plant toxin, rna n-glycosidase, antiviral protein |
| Biological source | Mirabilis jalapa (garden four-o'clock) |
| Total number of polymer chains | 4 |
| Total formula weight | 115899.62 |
| Authors | Nishida, N.,Ninomiya, Y.,Yoshida, T.,Habuka, N.,Tsuge, H. (deposition date: 2025-10-07, release date: 2025-12-03, Last modification date: 2026-01-07) |
| Primary citation | Nishida, N.,Ninomiya, Y.,Yoshida, T.,Tanzawa, T.,Maki, Y.,Yoshida, H.,Tsuge, H.,Habuka, N. Structure of Ribosome-Inactivating Protein from Mirabilis jalapa and Its L12-Stalk-Dependent Inhibition of Escherichia coli Ribosome. Toxins, 17:-, 2025 Cited by PubMed Abstract: antiviral protein (MAP) is the type I ribosome-inactivating protein (RIP), which consists of an RNA -glycosylase domain with no carbohydrate-binding domain. Unlike many RIPs, such as ricin or trichosanthin, which inactivate eukaryotic ribosomes, MAP also inactivates the ribosome by cleaving the -glycosidic bond at A2660 of 23S ribosomal RNA. The structure of the wild-type MAP has not been revealed yet. Here, we expressed, purified, and crystallized the plural recombinant MAPs, including both E168Q and R171Q mutations (MAP-EQRQ) in , and determined the crystal structure of MAP-EQRQ at 2.1 Å resolution. According to the predicted structure with RNA (sarcin-ricin loop) and the mutant protein's activities using quantitative RT-PCR, we showed that residue R171 at the active site of MAP is a key residue to form the stable complex with target adenine. Furthermore, we showed that MAP bound the C-terminal domains of eukaryotic P2-stalk as well as L12-stalk. PubMed: 41441611DOI: 10.3390/toxins17120575 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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