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protein Protein-protein interface(s) links
Viral protein PDB id
1ei7
Jmol
Contents
Protein chains
158 a.a. *
Waters ×334
* Residue conservation analysis
PDB id:
1ei7
Name: Viral protein
Title: Tmv coat protein refined from the 4-layer aggregate
Structure: Coat protein. Chain: a, b
Source: Tobacco mosaic virus. Organism_taxid: 12242
Resolution:
2.45Å     R-factor:   0.195     R-free:   0.225
Authors: B.Bhyravbhatla,S.J.Watowich,D.L.Caspar
Key ref: B.Bhyravbhatla et al. (1998). 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. PubMed id: 9449361 DOI: 10.1016/S0006-3495(98)77819-1
Date:
24-Feb-00     Release date:   12-Apr-00    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P69687  (CAPSD_TMV) -  Capsid protein
Seq:
Struc: 		159 a.a.
158 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     virion   2 terms 
  Biochemical function     structural molecule activity     1 term  

 

 
DOI no: 10.1016/S0006-3495(98)77819-1 Biophys J 74:604-615 (1998)
PubMed id: 9449361  
 
 
Refined atomic model of the four-layer aggregate of the tobacco mosaic virus coat protein at 2.4-A resolution.
B.Bhyravbhatla, S.J.Watowich, D.L.Caspar.
 
  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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20688511 C.M.Soto, and B.R.Ratna (2010).
Virus hybrids as nanomaterials for biotechnology.
  Curr Opin Biotechnol, 21, 426-438.  
20558300 D.K.Clare, and E.V.Orlova (2010).
4.6A Cryo-EM reconstruction of tobacco mosaic virus from images recorded at 300 keV on a 4k x 4k CCD camera.
  J Struct Biol, 171, 303-308.
PDB code: 2xea
18645236 C.L.Lawson, S.Dutta, J.D.Westbrook, K.Henrick, and H.M.Berman (2008).
Representation of viruses in the remediated PDB archive.
  Acta Crystallogr D Biol Crystallogr, 64, 874-882.  
18213477 S.Kasas, and G.Dietler (2008).
Probing nanomechanical properties from biomolecules to living cells.
  Pflugers Arch, 456, 13-27.  
18220254 S.W.Chung, A.D.Presley, S.Elhadj, S.Hok, S.S.Hah, A.A.Chernov, M.B.Francis, B.E.Eaton, D.L.Feldheim, and J.J.DeYoreo (2008).
Scanning probe-based fabrication of 3D nanostructures via affinity templates, functional RNA, and meniscus-mediated surface remodeling.
  Scanning, 30, 159-171.  
18498137 V.L.Morton, P.G.Stockley, N.J.Stonehouse, and A.E.Ashcroft (2008).
Insights into virus capsid assembly from non-covalent mass spectrometry.
  Mass Spectrom Rev, 27, 575-595.  
17371449 A.Schmatulla, N.Maghelli, and O.Marti (2007).
Micromechanical properties of tobacco mosaic viruses.
  J Microsc, 225, 264-268.  
17585939 C.Sachse, J.Z.Chen, P.D.Coureux, M.E.Stroupe, M.Fändrich, and N.Grigorieff (2007).
High-resolution electron microscopy of helical specimens: a fresh look at tobacco mosaic virus.
  J Mol Biol, 371, 812-835.
PDB code: 2om3
17493658 S.Asurmendi, R.H.Berg, T.J.Smith, M.Bendahmane, and R.N.Beachy (2007).
Aggregation of TMV CP plays a role in CP functions and in coat-protein-mediated resistance.
  Virology, 366, 98.  
16555353 K.Sugimoto, S.Kanamaru, K.Iwasaki, F.Arisaka, and I.Yamashita (2006).
Construction of a ball-and-spike protein supramolecule.
  Angew Chem Int Ed Engl, 45, 2725-2728.  
16506261 M.Endo, H.Wang, M.Fujitsuka, and T.Majima (2006).
Pyrene-stacked nanostructures constructed in the recombinant tobacco mosaic virus rod scaffold.
  Chemistry, 12, 3735-3740.  
16485991 K.Cahill (2005).
Helices in biomolecules.
  Phys Rev E Stat Nonlin Soft Matter Phys, 72, 062901.  
12899688 E.N.Dobrov, G.A.Badun, E.V.Lukashina, N.V.Fedorova, A.L.Ksenofontov, V.M.Fedoseev, and L.A.Baratova (2003).
Tritium planigraphy comparative structural study of tobacco mosaic virus and its mutant with altered host specificity.
  Eur J Biochem, 270, 3300-3308.  
  12818240 E.R.Rafikova, B.I.Kurganov, A.M.Arutyunyan, S.V.Kust, V.A.Drachev, and E.N.Dobrov (2003).
A mechanism of macroscopic (amorphous) aggregation of the tobacco mosaic virus coat protein.
  Int J Biochem Cell Biol, 35, 1452-1460.  
12147762 J.N.Culver (2002).
Tobacco mosaic virus assembly and disassembly: determinants in pathogenicity and resistance.
  Annu Rev Phytopathol, 40, 287-308.  
10212933 P.J.Butler (1999).
Self-assembly of tobacco mosaic virus: the role of an intermediate aggregate in generating both specificity and speed.
  Philos Trans R Soc Lond B Biol Sci, 354, 537-550.  
9449360 R.Díaz-Avalos, and D.L.Caspar (1998).
Structure of the stacked disk aggregate of tobacco mosaic virus protein.
  Biophys J, 74, 595-603.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.