1EI7

TMV COAT PROTEIN REFINED FROM THE 4-LAYER AGGREGATE

Summary for 1EI7

• Entry DOI: 10.2210/pdb1ei7/pdb
• Descriptor: COAT PROTEIN (2 entities in total)
• Functional Keywords: disordered loops, viral protein, virus
• Biological source: Tobacco mosaic virus
• Total number of polymer chains: 2
• Total formula weight: 35010.85

Authors

Bhyravbhatla, B.,Watowich, S.J.,Caspar, D.L. (deposition date: 2000-02-24, release date: 2000-04-12, Last modification date: 2024-02-07)

Primary citation

Bhyravbhatla, B.,Watowich, S.J.,Caspar, D.L.
Refined atomic model of the four-layer aggregate of the tobacco mosaic virus coat protein at 2.4-A resolution.
Biophys.J., 74:604-615, 1998

PubMed Abstract: Previous x-ray studies (2.8-A resolution) on crystals of tobacco mosaic virus coat protein grown from solutions containing high salt have characterized the structure of the protein aggregate as a dimer of a bilayered cylindrical disk formed by 34 chemically identical subunits. We have determined the crystal structure of the disk aggregate at 2.4-A resolution using x-ray diffraction from crystals maintained at cryogenic temperatures. Two regions of interest have been extensively refined. First, residues of the low-radius loop region, which were not modeled previously, have been traced completely in our electron density maps. Similar to the structure observed in the virus, the right radial helix in each protomer ends around residue 87, after which the protein chain forms an extended chain that extends to the left radial helix. The left radial helix appears as a long alpha-helix with high temperature factors for the main-chain atoms in the inner portion. The side-chain atoms in this region (residues 90-110) are not visible in the electron density maps and are assumed to be disordered. Second, interactions between subunits in the symmetry-related central A pair have been determined. No direct protein-protein interactions are observed in the major overlap region between these subunits; all interactions are mediated by two layers of ordered solvent molecules. The current structure emphasizes the importance of water in biological macromolecular assemblies.

PubMed: 9449361

Experimental method

X-RAY DIFFRACTION (2.45 Å)