| Structural highlights
Function
[POLG_TEV] Capsid protein: involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification.[1] [2] Nuclear inclusion protein B: an RNA-dependent RNA polymerase that plays an essential role in the virus replication.[3] [4] Helper component proteinase: required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity.[5] [6] Cytoplasmic inclusion protein: has helicase activity. It may be involved in replication.[7] [8] Both 6K peptides are indispensable for virus replication (By similarity).[9] [10] Nuclear inclusion protein A: has RNA-binding and proteolytic activities.[11] [12]
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
Because of its stringent sequence specificity, the 3C-type protease from tobacco etch virus (TEV) is frequently used to remove affinity tags from recombinant proteins. It is unclear, however, exactly how TEV protease recognizes its substrates with such high selectivity. The crystal structures of two TEV protease mutants, inactive C151A and autolysis-resistant S219D, have now been solved at 2.2- and 1.8-A resolution as complexes with a substrate and product peptide, respectively. The enzyme does not appear to have been perturbed by the mutations in either structure, and the modes of binding of the product and substrate are virtually identical. Analysis of the protein-ligand interactions helps to delineate the structural determinants of substrate specificity and provides guidance for reengineering the enzyme to further improve its utility for biotechnological applications.
Structural basis for the substrate specificity of tobacco etch virus protease.,Phan J, Zdanov A, Evdokimov AG, Tropea JE, Peters HK 3rd, Kapust RB, Li M, Wlodawer A, Waugh DS J Biol Chem. 2002 Dec 27;277(52):50564-72. Epub 2002 Oct 10. PMID:12377789[13]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Blanc S, Ammar ED, Garcia-Lampasona S, Dolja VV, Llave C, Baker J, Pirone TP. Mutations in the potyvirus helper component protein: effects on interactions with virions and aphid stylets. J Gen Virol. 1998 Dec;79 ( Pt 12):3119-22. PMID:9880030
- ↑ Kasschau KD, Carrington JC. Long-distance movement and replication maintenance functions correlate with silencing suppression activity of potyviral HC-Pro. Virology. 2001 Jun 20;285(1):71-81. PMID:11414807 doi:http://dx.doi.org/10.1006/viro.2001.0901
- ↑ Blanc S, Ammar ED, Garcia-Lampasona S, Dolja VV, Llave C, Baker J, Pirone TP. Mutations in the potyvirus helper component protein: effects on interactions with virions and aphid stylets. J Gen Virol. 1998 Dec;79 ( Pt 12):3119-22. PMID:9880030
- ↑ Kasschau KD, Carrington JC. Long-distance movement and replication maintenance functions correlate with silencing suppression activity of potyviral HC-Pro. Virology. 2001 Jun 20;285(1):71-81. PMID:11414807 doi:http://dx.doi.org/10.1006/viro.2001.0901
- ↑ Blanc S, Ammar ED, Garcia-Lampasona S, Dolja VV, Llave C, Baker J, Pirone TP. Mutations in the potyvirus helper component protein: effects on interactions with virions and aphid stylets. J Gen Virol. 1998 Dec;79 ( Pt 12):3119-22. PMID:9880030
- ↑ Kasschau KD, Carrington JC. Long-distance movement and replication maintenance functions correlate with silencing suppression activity of potyviral HC-Pro. Virology. 2001 Jun 20;285(1):71-81. PMID:11414807 doi:http://dx.doi.org/10.1006/viro.2001.0901
- ↑ Blanc S, Ammar ED, Garcia-Lampasona S, Dolja VV, Llave C, Baker J, Pirone TP. Mutations in the potyvirus helper component protein: effects on interactions with virions and aphid stylets. J Gen Virol. 1998 Dec;79 ( Pt 12):3119-22. PMID:9880030
- ↑ Kasschau KD, Carrington JC. Long-distance movement and replication maintenance functions correlate with silencing suppression activity of potyviral HC-Pro. Virology. 2001 Jun 20;285(1):71-81. PMID:11414807 doi:http://dx.doi.org/10.1006/viro.2001.0901
- ↑ Blanc S, Ammar ED, Garcia-Lampasona S, Dolja VV, Llave C, Baker J, Pirone TP. Mutations in the potyvirus helper component protein: effects on interactions with virions and aphid stylets. J Gen Virol. 1998 Dec;79 ( Pt 12):3119-22. PMID:9880030
- ↑ Kasschau KD, Carrington JC. Long-distance movement and replication maintenance functions correlate with silencing suppression activity of potyviral HC-Pro. Virology. 2001 Jun 20;285(1):71-81. PMID:11414807 doi:http://dx.doi.org/10.1006/viro.2001.0901
- ↑ Blanc S, Ammar ED, Garcia-Lampasona S, Dolja VV, Llave C, Baker J, Pirone TP. Mutations in the potyvirus helper component protein: effects on interactions with virions and aphid stylets. J Gen Virol. 1998 Dec;79 ( Pt 12):3119-22. PMID:9880030
- ↑ Kasschau KD, Carrington JC. Long-distance movement and replication maintenance functions correlate with silencing suppression activity of potyviral HC-Pro. Virology. 2001 Jun 20;285(1):71-81. PMID:11414807 doi:http://dx.doi.org/10.1006/viro.2001.0901
- ↑ Phan J, Zdanov A, Evdokimov AG, Tropea JE, Peters HK 3rd, Kapust RB, Li M, Wlodawer A, Waugh DS. Structural basis for the substrate specificity of tobacco etch virus protease. J Biol Chem. 2002 Dec 27;277(52):50564-72. Epub 2002 Oct 10. PMID:12377789 doi:http://dx.doi.org/10.1074/jbc.M207224200
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