2TMV
VISUALIZATION OF PROTEIN-NUCLEIC ACID INTERACTIONS IN A VIRUS. REFINED STRUCTURE OF INTACT TOBACCO MOSAIC VIRUS AT 2.9 ANGSTROMS RESOLUTION BY X-RAY FIBER DIFFRACTION
Summary for 2TMV
| Entry DOI | 10.2210/pdb2tmv/pdb |
| Descriptor | RNA (5'-R(P*GP*AP*A)-3'), TMV COAT PROTEIN, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | virus, helical virus, virus-rna complex, virus/rna |
| Biological source | Tobacco mosaic virus |
| Total number of polymer chains | 2 |
| Total formula weight | 18504.16 |
| Authors | Stubbs, G.,Pattanayek, R.,Namba, K. (deposition date: 1988-09-15, release date: 1989-01-09, Last modification date: 2024-02-21) |
| Primary citation | Namba, K.,Pattanayek, R.,Stubbs, G. Visualization of protein-nucleic acid interactions in a virus. Refined structure of intact tobacco mosaic virus at 2.9 A resolution by X-ray fiber diffraction. J.Mol.Biol., 208:307-325, 1989 Cited by PubMed Abstract: The structure of tobacco mosaic virus (TMV) has been determined by fiber diffraction methods at 2.9 A resolution, and refined by restrained least-squares to an R-factor of 0.096. Protein-nucleic acid interactions are clearly visible. The final model contains all of the non-hydrogen atoms of the RNA and the protein, 71 water molecules, and two calcium-binding sites. Viral disassembly is driven by electrostatic repulsions between the charges in two carboxyl-carboxylate pairs and a phosphate-carboxylate pair. The phosphate-carboxylate pair and at least one of the carboxyl-carboxylate pairs appear to be calcium-binding sites. Nucleotide specificity, enabling TMV to recognize its own RNA by a repeating pattern of guanine residues, is provided by two guanine-specific hydrogen bonds in one of the three base-binding sites. PubMed: 2769760DOI: 10.1016/0022-2836(89)90391-4 PDB entries with the same primary citation |
| Experimental method | FIBER DIFFRACTION (2.9 Å) |
Structure validation
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