<table><tr><td colspan='2'>[[2cse]] is a 27 chain structure with sequence from [http://en.wikipedia.org/wiki/Mammalian_orthoreovirus_1 Mammalian orthoreovirus 1] and [http://en.wikipedia.org/wiki/Mammalian_orthoreovirus_3 Mammalian orthoreovirus 3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CSE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CSE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2cse]] is a 27 chain structure with sequence from [https://en.wikipedia.org/wiki/Mammalian_orthoreovirus_1_Lang Mammalian orthoreovirus 1 Lang] and [https://en.wikipedia.org/wiki/Mammalian_orthoreovirus_3_Dearing Mammalian orthoreovirus 3 Dearing]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CSE FirstGlance]. <br>
[[http://www.uniprot.org/uniprot/LMBD1_REOVL LMBD1_REOVL]] Inner capsid (core) component. Displays NTPase, RNA 5'-triphosphatase (RTPase) and RNA helicase activities and probably participates in transcription of the viral genome. Helicase activity might be involved in unwinding or reannealing dsRNA during RNA synthesis. RTPase enzymatic activity represents the first step in RNA capping, which yields a 5'-diphosphorylated plus-strand RNA (By similarity). [[http://www.uniprot.org/uniprot/MU1_REOVL MU1_REOVL]] Major outer capsid protein involved in host cell membrane penetration. In the endocytic compartment, outer-capsid protein sigma-3 is removed by cathepsin proteases, which exposes the viral membrane-penetration protein mu-1. Both myristoylated peptides mu-1N and phi are released during infectious subvirion particles (ISVP) formation in the endosome. They associate with host membranes and mu-1N induces permeabilization and delivery of transcriptionally active viral particles into the host cell cytoplasm. Seems to induce apoptosis in the host cell.<ref>PMID:11007773</ref> <ref>PMID:15280481</ref> <ref>PMID:16912293</ref> <ref>PMID:17005655</ref> <ref>PMID:18369316</ref> The viral outer shell polypeptides, of which mu-1 is one, impose structural constraints that prevent elongation of nascent transcripts by the RNA-dependent RNA polymerase lambda-3.<ref>PMID:11007773</ref> <ref>PMID:15280481</ref> <ref>PMID:16912293</ref> <ref>PMID:17005655</ref> <ref>PMID:18369316</ref> [[http://www.uniprot.org/uniprot/LMBD2_REOVD LMBD2_REOVD]] Outer capsid protein involved in mRNA capping. Catalyzes the last 3 enzymatic activities for formation of the 5' cap structure on the viral plus-strand transcripts, namely the RNA guanylyltransferase, RNA-7N- and RNA-2'O-methyltransferase activities. [[http://www.uniprot.org/uniprot/SIGM3_REOVL SIGM3_REOVL]] Stimulates translation by blocking the activation of the dsRNA-dependent protein kinase EIF2AK2/PKR, thereby inhibiting the host interferon response. Sigma3 prevents the activation of EIF2AK2 by competing with the kinase for dsRNA-binding (By similarity). The viral outer shell polypeptides, of which sigma-3 is one, impose structural constraints that prevent elongation of nascent transcripts by the RNA-dependent RNA polymerase lambda-3. [[http://www.uniprot.org/uniprot/SIGM2_REOVL SIGM2_REOVL]] Inner capsid (core) component.
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[https://www.uniprot.org/uniprot/MU1_REOVL MU1_REOVL] Major outer capsid protein involved in host cell membrane penetration. In the endocytic compartment, outer-capsid protein sigma-3 is removed by cathepsin proteases, which exposes the viral membrane-penetration protein mu-1. Both myristoylated peptides mu-1N and phi are released during infectious subvirion particles (ISVP) formation in the endosome. They associate with host membranes and mu-1N induces permeabilization and delivery of transcriptionally active viral particles into the host cell cytoplasm. Seems to induce apoptosis in the host cell.<ref>PMID:11007773</ref> <ref>PMID:15280481</ref> <ref>PMID:16912293</ref> <ref>PMID:17005655</ref> <ref>PMID:18369316</ref> The viral outer shell polypeptides, of which mu-1 is one, impose structural constraints that prevent elongation of nascent transcripts by the RNA-dependent RNA polymerase lambda-3.<ref>PMID:11007773</ref> <ref>PMID:15280481</ref> <ref>PMID:16912293</ref> <ref>PMID:17005655</ref> <ref>PMID:18369316</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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Line 19:
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2cse ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2cse ConSurf].
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== Publication Abstract from PubMed ==
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Reovirus is a useful model for addressing the molecular basis of membrane penetration by one of the larger nonenveloped animal viruses. We now report the structure of the reovirus virion at approximately 7.0 A resolution as obtained by electron cryomicroscopy and three-dimensional image reconstruction. Several features of the myristoylated outer capsid protein mu1, not seen in a previous X-ray crystal structure of the mu1-sigma3 heterohexamer, are evident in the virion. These features appear to be important for stabilizing the outer capsid, regulating the conformational changes in mu1 that accompany perforation of target membranes, and contributing directly to membrane penetration during cell entry.
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Features of reovirus outer capsid protein mu1 revealed by electron cryomicroscopy and image reconstruction of the virion at 7.0 Angstrom resolution.,Zhang X, Ji Y, Zhang L, Harrison SC, Marinescu DC, Nibert ML, Baker TS Structure. 2005 Oct;13(10):1545-57. PMID:16216585<ref>PMID:16216585</ref>
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==See Also==
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*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
MU1_REOVL Major outer capsid protein involved in host cell membrane penetration. In the endocytic compartment, outer-capsid protein sigma-3 is removed by cathepsin proteases, which exposes the viral membrane-penetration protein mu-1. Both myristoylated peptides mu-1N and phi are released during infectious subvirion particles (ISVP) formation in the endosome. They associate with host membranes and mu-1N induces permeabilization and delivery of transcriptionally active viral particles into the host cell cytoplasm. Seems to induce apoptosis in the host cell.[1][2][3][4][5] The viral outer shell polypeptides, of which mu-1 is one, impose structural constraints that prevent elongation of nascent transcripts by the RNA-dependent RNA polymerase lambda-3.[6][7][8][9][10]
Evolutionary Conservation
Checkto colour the structure by Evolutionary Conservation, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
↑ Farsetta DL, Chandran K, Nibert ML. Transcriptional activities of reovirus RNA polymerase in recoated cores. Initiation and elongation are regulated by separate mechanisms. J Biol Chem. 2000 Dec 15;275(50):39693-701. PMID:11007773 doi:http://dx.doi.org/10.1074/jbc.M004562200
↑ Odegard AL, Chandran K, Zhang X, Parker JS, Baker TS, Nibert ML. Putative autocleavage of outer capsid protein micro1, allowing release of myristoylated peptide micro1N during particle uncoating, is critical for cell entry by reovirus. J Virol. 2004 Aug;78(16):8732-45. PMID:15280481 doi:http://dx.doi.org/10.1128/JVI.78.16.8732-8745.2004
↑ Coffey CM, Sheh A, Kim IS, Chandran K, Nibert ML, Parker JS. Reovirus outer capsid protein micro1 induces apoptosis and associates with lipid droplets, endoplasmic reticulum, and mitochondria. J Virol. 2006 Sep;80(17):8422-38. PMID:16912293 doi:http://dx.doi.org/80/17/8422
↑ Ivanovic T, Agosto MA, Zhang L, Chandran K, Harrison SC, Nibert ML. Peptides released from reovirus outer capsid form membrane pores that recruit virus particles. EMBO J. 2008 Apr 23;27(8):1289-98. Epub 2008 Mar 27. PMID:18369316 doi:http://dx.doi.org/emboj200860
↑ Farsetta DL, Chandran K, Nibert ML. Transcriptional activities of reovirus RNA polymerase in recoated cores. Initiation and elongation are regulated by separate mechanisms. J Biol Chem. 2000 Dec 15;275(50):39693-701. PMID:11007773 doi:http://dx.doi.org/10.1074/jbc.M004562200
↑ Odegard AL, Chandran K, Zhang X, Parker JS, Baker TS, Nibert ML. Putative autocleavage of outer capsid protein micro1, allowing release of myristoylated peptide micro1N during particle uncoating, is critical for cell entry by reovirus. J Virol. 2004 Aug;78(16):8732-45. PMID:15280481 doi:http://dx.doi.org/10.1128/JVI.78.16.8732-8745.2004
↑ Coffey CM, Sheh A, Kim IS, Chandran K, Nibert ML, Parker JS. Reovirus outer capsid protein micro1 induces apoptosis and associates with lipid droplets, endoplasmic reticulum, and mitochondria. J Virol. 2006 Sep;80(17):8422-38. PMID:16912293 doi:http://dx.doi.org/80/17/8422
↑ Ivanovic T, Agosto MA, Zhang L, Chandran K, Harrison SC, Nibert ML. Peptides released from reovirus outer capsid form membrane pores that recruit virus particles. EMBO J. 2008 Apr 23;27(8):1289-98. Epub 2008 Mar 27. PMID:18369316 doi:http://dx.doi.org/emboj200860
