8a5t: Difference between revisions

Revision as of 12:59, 20 December 2023

Capsid structure of the L-A helper virus from native viral communitiesCapsid structure of the L-A helper virus from native viral communities

Structural highlights

8a5t is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.78Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GAG_SCVLA Capsid protein self-assembles to form an icosahedral capsid with a T=2 symmetry, 40 nm in diameter, and consisting of 60 capsid proteins asymmetric dimers. The capsid encapsulates the genomic dsRNA and the polymerase and remains intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nacent transcripts are transcribed within the structural confines of the virion and are extruded into the cytoplasm.^[1] ^[2] Binds and removes 5' cap structures from cellular mRNA. Forms a covalent bond with m7GMP through His-154 of the capsid protein while releasing the mRNA body.^[3] ^[4]

References

↑ Blanc A, Goyer C, Sonenberg N. The coat protein of the yeast double-stranded RNA virus L-A attaches covalently to the cap structure of eukaryotic mRNA. Mol Cell Biol. 1992 Aug;12(8):3390-8. PMID:1630453
↑ Masison DC, Blanc A, Ribas JC, Carroll K, Sonenberg N, Wickner RB. Decoying the cap- mRNA degradation system by a double-stranded RNA virus and poly(A)- mRNA surveillance by a yeast antiviral system. Mol Cell Biol. 1995 May;15(5):2763-71. PMID:7739557
↑ Blanc A, Goyer C, Sonenberg N. The coat protein of the yeast double-stranded RNA virus L-A attaches covalently to the cap structure of eukaryotic mRNA. Mol Cell Biol. 1992 Aug;12(8):3390-8. PMID:1630453
↑ Masison DC, Blanc A, Ribas JC, Carroll K, Sonenberg N, Wickner RB. Decoying the cap- mRNA degradation system by a double-stranded RNA virus and poly(A)- mRNA surveillance by a yeast antiviral system. Mol Cell Biol. 1995 May;15(5):2763-71. PMID:7739557

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OCA

[1] Blanc A, Goyer C, Sonenberg N. The coat protein of the yeast double-stranded RNA virus L-A attaches covalently to the cap structure of eukaryotic mRNA. Mol Cell Biol. 1992 Aug;12(8):3390-8. PMID:1630453

[2] Masison DC, Blanc A, Ribas JC, Carroll K, Sonenberg N, Wickner RB. Decoying the cap- mRNA degradation system by a double-stranded RNA virus and poly(A)- mRNA surveillance by a yeast antiviral system. Mol Cell Biol. 1995 May;15(5):2763-71. PMID:7739557

[3] Blanc A, Goyer C, Sonenberg N. The coat protein of the yeast double-stranded RNA virus L-A attaches covalently to the cap structure of eukaryotic mRNA. Mol Cell Biol. 1992 Aug;12(8):3390-8. PMID:1630453

[4] Masison DC, Blanc A, Ribas JC, Carroll K, Sonenberg N, Wickner RB. Decoying the cap- mRNA degradation system by a double-stranded RNA virus and poly(A)- mRNA surveillance by a yeast antiviral system. Mol Cell Biol. 1995 May;15(5):2763-71. PMID:7739557

[1]

[2]

[3]

[4]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8a5t is ON HOLD  until Paper Publication
+==Capsid structure of the L-A helper virus from native viral communities==
+<StructureSection load='8a5t' size='340' side='right'caption='[[8a5t]], [[Resolution|resolution]] 3.78&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8a5t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8A5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A5T FirstGlance]. <br>
-Description:
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.78&#8491;</td></tr>
-[[Category: Unreleased Structures]]
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8a5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a5t OCA], [https://pdbe.org/8a5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a5t RCSB], [https://www.ebi.ac.uk/pdbsum/8a5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a5t ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/GAG_SCVLA GAG_SCVLA] Capsid protein self-assembles to form an icosahedral capsid with a T=2 symmetry, 40 nm in diameter, and consisting of 60 capsid proteins asymmetric dimers. The capsid encapsulates the genomic dsRNA and the polymerase and remains intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nacent transcripts are transcribed within the structural confines of the virion and are extruded into the cytoplasm.<ref>PMID:1630453</ref> <ref>PMID:7739557</ref>   Binds and removes 5' cap structures from cellular mRNA. Forms a covalent bond with m7GMP through His-154 of the capsid protein while releasing the mRNA body.<ref>PMID:1630453</ref> <ref>PMID:7739557</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Saccharomyces cerevisiae]]
+[[Category: Kastritis PL]]
+[[Category: Schmidt L]]
+[[Category: Stubbs MT]]
+[[Category: Tueting C]]

8a5t: Difference between revisions

Revision as of 12:59, 20 December 2023

Capsid structure of the L-A helper virus from native viral communitiesCapsid structure of the L-A helper virus from native viral communities

Structural highlights

Function

References

Contents

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8a5t: Difference between revisions

Revision as of 12:59, 20 December 2023

Capsid structure of the L-A helper virus from native viral communitiesCapsid structure of the L-A helper virus from native viral communities

Structural highlights

Function

References

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