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

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: 2769760
DOI: 10.1016/0022-2836(89)90391-4

Experimental method

FIBER DIFFRACTION (2.9 Å)