1ei7 | pdb_00001ei7

TMV COAT PROTEIN REFINED FROM THE 4-LAYER AGGREGATE

spinqualitylabelsall models 1ei7, resolution 2.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ei7 is a 2 chain structure with sequence from Tobacco mosaic virus. The January 2009 RCSB PDB Molecule of the Month feature on Tobacco Mosaic Virus by David Goodsell is 10.2210/rcsb_pdb/mom_2009_1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CAPSD_TMV] Capsid protein self-assembles to form rod-shaped virions about 18 nm in diameter with a central canal enclosing the viral genomic RNA. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Refined atomic model of the four-layer aggregate of the tobacco mosaic virus coat protein at 2.4-A resolution.,Bhyravbhatla B, Watowich SJ, Caspar DL Biophys J. 1998 Jan;74(1):604-15. PMID:9449361 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Tobacco Mosaic Virus Virus coat proteins 3D structures

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