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InterPro: IPR001337 Tobacco mosaic virus-like, coat protein

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UniProtKB
Matches:
438 proteins
AccessionHelp IPR001337 TMV-like_coat
TypeHelp Family
SignaturesHelp
GO Term annotationHelp
Function GO:0005198 structural molecule activity
Component GO:0019028 viral capsid
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This family contains coat proteins from tobamoviruses, which are ssRNA positive-strand viruses with no DNA stage. Examples include Tobacco mosaic virus (TMV), Cucumber green mottle mosaic virus and Ribgrass mosaic virus (RMV).

In order to establish infections, viruses must be delivered to the cells of potential hosts and must then engage in activities that enable their genomes to be expressed and replicated. With most viruses, the events that precede the onset of production of progeny virus particles are referred to as the early events and, in the case of positive-strand RNA viruses, they include the initial interaction with and entry of host cells and the release (uncoating) of the genome from the virus particles. The uncoating process in TMV may involve the bidirectional release of coat protein subunits from the viral RNA which may be mediated by cotranslational and coreplicational disassembly mechanisms [1].

The TMV particle is assembled from its constituent coat protein and RNA by a complex process. The protein forms an obligatory intermediate (a cylindrical disk composed of two layers of protein units), which recognises a specific RNA hairpin sequence. This mechanism simultaneously fulfils the physical requirement for nucleating the growth of the helical particle and the biological requirement for specific recognition of the viral DNA [2].

Structural linksHelp
SCOP: a.24.5.1
CATH: 1.20.120.70
Database linksHelp
PANDIT: PF00721
Blocks: IPB001337

Taxonomic coverageHelp

Example proteinsHelp
P03579 Coat protein

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Example Proteins Key


InterPro entry accession number/name and structure databases Colour code

PublicationsHelp
1. Shaw JG.
Tobacco mosaic virus and the study of early events in virus infections.
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 354 603-11 1999 [PubMed: 10212940]
http://dx.doi.org/10.1098/rstb.1999.0412
2. Klug A.
The tobacco mosaic virus particle: structure and assembly.
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 354 531-5 1999 [PubMed: 10212932]
http://dx.doi.org/10.1098/rstb.1999.0404

Additional ReadingHelp
Pattanayek R, Stubbs G.
Structure of the U2 strain of tobacco mosaic virus refined at 3.5 A resolution using X-ray fiber diffraction.
J. Mol. Biol. 228 1992 516-28 [PubMed: 1453461]
http://dx.doi.org/10.1016/0022-2836(92)90839-C
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 1989 307-25 [PubMed: 2769760]
http://dx.doi.org/10.1016/0022-2836(89)90391-4
Wang H, Stubbs G.
Molecular dynamics in refinement against fiber diffraction data.
Acta Crystallogr., A, Found. Crystallogr. 49 1993 504-13 [PubMed: 8129880]
http://dx.doi.org/10.1107/S0108767392011255
Wang H, Stubbs G.
Structure determination of cucumber green mottle mosaic virus by X-ray fiber diffraction. Significance for the evolution of tobamoviruses.
J. Mol. Biol. 239 1994 371-84 [PubMed: 8201619]
http://dx.doi.org/10.1006/jmbi.1994.1379
Bhyravbhatla B, Watowich SJ, Caspar DL.
Refined atomic model of the four-layer aggregate of the tobacco mosaic virus coat protein at 2.4-A resolution.
Biophys. J. 74 1998 604-15 [PubMed: 9449361]
http://www.biophysj.org/cgi/content/abstract/74/1/604
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InterPro 23.1