2cse: Difference between revisions

Latest revision as of 12:18, 14 February 2024

Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A ResolutionFeatures of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution

2cse, resolution 7.00Å

Structural highlights

2cse is a 27 chain structure with sequence from Mammalian orthoreovirus 1 Lang and Mammalian orthoreovirus 3 Dearing. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 7Å
Experimental data:	Check
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ 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
↑ Zhang L, Chandran K, Nibert ML, Harrison SC. Reovirus mu1 structural rearrangements that mediate membrane penetration. J Virol. 2006 Dec;80(24):12367-76. Epub 2006 Sep 27. PMID:17005655 doi:http://dx.doi.org/10.1128/JVI.01343-06
↑ 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
↑ Zhang L, Chandran K, Nibert ML, Harrison SC. Reovirus mu1 structural rearrangements that mediate membrane penetration. J Virol. 2006 Dec;80(24):12367-76. Epub 2006 Sep 27. PMID:17005655 doi:http://dx.doi.org/10.1128/JVI.01343-06
↑ 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

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OCA

[1] 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

[2] 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

[3] 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

[4] Zhang L, Chandran K, Nibert ML, Harrison SC. Reovirus mu1 structural rearrangements that mediate membrane penetration. J Virol. 2006 Dec;80(24):12367-76. Epub 2006 Sep 27. PMID:17005655 doi:http://dx.doi.org/10.1128/JVI.01343-06

[5] 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

[6] 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

[7] 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

[8] 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

[9] Zhang L, Chandran K, Nibert ML, Harrison SC. Reovirus mu1 structural rearrangements that mediate membrane penetration. J Virol. 2006 Dec;80(24):12367-76. Epub 2006 Sep 27. PMID:17005655 doi:http://dx.doi.org/10.1128/JVI.01343-06

[10] 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

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@@ Line 1: / Line 1: @@
-[[Image:2cse.png|left|200px]]
-{{STRUCTURE_2cse|  PDB=2cse  |  SCENE=  }}
+==Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution==
+<SX load='2cse' size='340' side='right' viewer='molstar' caption='[[2cse]], [[Resolution|resolution]] 7.00&Aring;' scene=''>
+== Structural highlights ==
+<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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 7&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cse OCA], [https://pdbe.org/2cse PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cse RCSB], [https://www.ebi.ac.uk/pdbsum/2cse PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cse ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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 ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cs/2cse_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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].
+<div style="clear:both"></div>
-===Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution===
+==See Also==
+*[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]]
-{{ABSTRACT_PUBMED_16216585}}
+== References ==
+<references/>
-==About this Structure==
+__TOC__
-[[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].
+</SX>
+[[Category: Large Structures]]
-==Reference==
+[[Category: Mammalian orthoreovirus 1 Lang]]
-<ref group="xtra">PMID:016216585</ref><references group="xtra"/>
+[[Category: Mammalian orthoreovirus 3 Dearing]]
-[[Category: Mammalian orthoreovirus 1]]
+[[Category: Baker TS]]
-[[Category: Mammalian orthoreovirus 3]]
+[[Category: Harrison SC]]
-[[Category: Baker, T S.]]
+[[Category: Ji Y]]
-[[Category: Harrison, S C.]]
+[[Category: Marinescu DC]]
-[[Category: Ji, Y.]]
+[[Category: Nibert ML]]
-[[Category: Marinescu, D C.]]
+[[Category: Zhang L]]
-[[Category: Nibert, M L.]]
+[[Category: Zhang X]]
-[[Category: Zhang, L.]]
-[[Category: Zhang, X.]]
-[[Category: Cryoem]]
-[[Category: Icosahedral virus]]
-[[Category: Image processing]]
-[[Category: Membrane penetration protein]]
-[[Category: Reovirus]]
-[[Category: Virus]]

2cse: Difference between revisions

Latest revision as of 12:18, 14 February 2024

Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A ResolutionFeatures of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution

Structural highlights

Function

Evolutionary Conservation

See Also

References

Contents

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2cse: Difference between revisions

Latest revision as of 12:18, 14 February 2024

Features of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A ResolutionFeatures of Reovirus Outer-Capsid Protein mu1 Revealed by Electron and Image Reconstruction of the virion at 7.0-A Resolution

Structural highlights

Function

Evolutionary Conservation

See Also

References

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