5tc1 - Revision history

OCA at 15:39, 6 March 2024

2024-03-06T15:39:30Z

←Older revision		Revision as of 15:39, 6 March 2024
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	<SX load='5tc1' size='340' side='right' viewer='molstar' caption='[[5tc1]], [[Resolution\|resolution]] 3.60Å' scene=''>		<SX load='5tc1' size='340' side='right' viewer='molstar' caption='[[5tc1]], [[Resolution\|resolution]] 3.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5tc1]] is a 10 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Enterobacteria_phage_ms2 Enterobacteria phage ms2~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TC1 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5TC1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5tc1]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_MS2 Escherichia virus MS2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TC1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TC1 FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">[[~~2ms2~~\|~~2ms2~~]]</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution\|Resolution]] 3.6Å</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5tc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tc1 OCA], [~~http~~://pdbe.org/5tc1 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5tc1 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5tc1 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5tc1 ProSAT]</span></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=5tc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tc1 OCA], [https://pdbe.org/5tc1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tc1 RCSB], [https://www.ebi.ac.uk/pdbsum/5tc1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tc1 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/CAPSD_BPMS2 CAPSD_BPMS2]] Self-assembles to form the T=3 icosahedral virus shell that protects the viral nucleic acid. Acts as a translational repressor by binding with high specificity to a single stem-loop structure in the genomic RNA that contains the initiation codon of the gene for the viral replicase. Involved in virus assembly through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome.<ref>PMID:16531233</ref> <ref>PMID:18662904</ref> <ref>PMID:26608810</ref> <ref>PMID:8254664</ref> <ref>PMID:9245600</ref> <ref>PMID:9469847</ref> [[http://www.uniprot.org/uniprot/MAT_BPMS2 MAT_BPMS2]] The maturation protein is required for the typical attachment of the phage to the side of the bacterial pili (PubMed:23810697). MP binds to sequences located toward each end of the genome, hence circularizing it (PubMed:26608810). The RNA genome-MP complex is released from the capsid upon host receptor binding (PubMed:23810697). MP enters the cell along with the viral RNA (PubMed:4551992).<ref>PMID:23810697</ref> <ref>PMID:26608810</ref> <ref>PMID:4551992</ref>	+	[https://www.uniprot.org/uniprot/CAPSD_BPMS2 CAPSD_BPMS2] Self-assembles to form the T=3 icosahedral virus shell that protects the viral nucleic acid. Acts as a translational repressor by binding with high specificity to a single stem-loop structure in the genomic RNA that contains the initiation codon of the gene for the viral replicase. Involved in virus assembly through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome.<ref>PMID:16531233</ref> <ref>PMID:18662904</ref> <ref>PMID:26608810</ref> <ref>PMID:8254664</ref> <ref>PMID:9245600</ref> <ref>PMID:9469847</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Packaging of the genome into a protein capsid and its subsequent delivery into a host cell are two fundamental processes in the life cycle of a virus. Unlike double-stranded DNA viruses, which pump their genome into a preformed capsid, single-stranded RNA (ssRNA) viruses, such as bacteriophage MS2, co-assemble their capsid with the genome; however, the structural basis of this co-assembly is poorly understood. MS2 infects Escherichia coli via the host 'sex pilus' (F-pilus); it was the first fully sequenced organism and is a model system for studies of translational gene regulation, RNA-protein interactions, and RNA virus assembly. Its positive-sense ssRNA genome of 3,569 bases is enclosed in a capsid with one maturation protein monomer and 89 coat protein dimers arranged in a T = 3 icosahedral lattice. The maturation protein is responsible for attaching the virus to an F-pilus and delivering the viral genome into the host during infection, but how the genome is organized and delivered is not known. Here we describe the MS2 structure at 3.6 A resolution, determined by electron-counting cryo-electron microscopy (cryoEM) and asymmetric reconstruction. We traced approximately 80% of the backbone of the viral genome, built atomic models for 16 RNA stem-loops, and identified three conserved motifs of RNA-coat protein interactions among 15 of these stem-loops with diverse sequences. The stem-loop at the 3' end of the genome interacts extensively with the maturation protein, which, with just a six-helix bundle and a six-stranded beta-sheet, forms a genome-delivery apparatus and joins 89 coat protein dimers to form a capsid. This atomic description of genome-capsid interactions in a spherical ssRNA virus provides insight into genome delivery via the host sex pilus and mechanisms underlying ssRNA-capsid co-assembly, and inspires speculation about the links between nucleoprotein complexes and the origins of viruses.	+
-		+
-	In situ structures of the genome and genome-delivery apparatus in a single-stranded RNA virus.,Dai X, Li Z, Lai M, Shu S, Du Y, Zhou ZH, Sun R Nature. 2017 Jan 5;541(7635):112-116. doi: 10.1038/nature20589. Epub 2016 Dec 19. PMID:27992877<ref>PMID:27992877</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 5tc1" style="background-color:#fffaf0;"></div>~~	+
-		+
-	~~==See Also==~~	+
-	*[[Virus coat proteins 3D structures\|Virus coat proteins 3D structures]]	+
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</SX>		</SX>
-	[[Category: ~~Enterobacteria phage ms2~~]]	+	[[Category: Escherichia virus MS2]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Dai~~, X H~~]]	+	[[Category: Dai XH]]
-	[[Category: Du~~, Y S~~]]	+	[[Category: Du YS]]
-	[[Category: Lai, M]]	+	[[Category: Lai M]]
-	[[Category: Li~~, Z H~~]]	+	[[Category: Li ZH]]
-	[[Category: Shu, S]]	+	[[Category: Shu S]]
-	[[Category: Sun, R]]	+	[[Category: Sun R]]
-	[[Category: Zhou~~, Z H]]~~	+	[[Category: Zhou ZH]]
-	~~[[Category: Asymmetric cryoem reconstruction]]~~	+
-	~~[[Category: Genome-capsid interaction]]~~	+
-	~~[[Category: Genome-delivery apparatus]]~~	+
-	~~[[Category: Ssrna genome structure]]~~	+
-	~~[[Category: Viral protein-rna complex~~]]	+

OCA at 21:43, 10 April 2020

2020-04-10T21:43:46Z

←Older revision		Revision as of 21:43, 10 April 2020
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	<SX load='5tc1' size='340' side='right' viewer='molstar' caption='[[5tc1]], [[Resolution\|resolution]] 3.60Å' scene=''>		<SX load='5tc1' size='340' side='right' viewer='molstar' caption='[[5tc1]], [[Resolution\|resolution]] 3.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5tc1]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_ms2 Enterobacteria phage ms2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TC1 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5TC1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5tc1]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_ms2 Enterobacteria phage ms2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TC1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5TC1 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2ms2\|2ms2]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2ms2\|2ms2]]</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5tc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tc1 OCA], [http://pdbe.org/5tc1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tc1 RCSB], [http://www.ebi.ac.uk/pdbsum/5tc1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tc1 ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5tc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tc1 OCA], [http://pdbe.org/5tc1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tc1 RCSB], [http://www.ebi.ac.uk/pdbsum/5tc1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tc1 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 20:		Line 20:

	==See Also==		==See Also==
-	*[[Virus coat ~~protein~~\|Virus coat ~~protein~~]]	+	*[[Virus coat proteins 3D structures\|Virus coat proteins 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 19:35, 6 March 2020

2020-03-06T19:35:59Z

←Older revision		Revision as of 19:35, 6 March 2020
Line 1:		Line 1:

	==In situ structures of the genome and genome-delivery apparatus in ssRNA bacteriophage MS2==		==In situ structures of the genome and genome-delivery apparatus in ssRNA bacteriophage MS2==
-	<~~StructureSection~~ load='5tc1' size='340' side='right' caption='[[5tc1]], [[Resolution\|resolution]] 3.60Å' scene=''>	+	<SX load='5tc1' size='340' side='right' viewer='molstar' caption='[[5tc1]], [[Resolution\|resolution]] 3.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5tc1]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_ms2 Enterobacteria phage ms2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TC1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TC1 FirstGlance]. <br>		<table><tr><td colspan='2'>[[5tc1]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_ms2 Enterobacteria phage ms2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TC1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TC1 FirstGlance]. <br>
Line 24:		Line 24:
	<references/>		<references/>
	__TOC__		__TOC__
-	</~~StructureSection~~>	+	</SX>
	[[Category: Enterobacteria phage ms2]]		[[Category: Enterobacteria phage ms2]]
		+	[[Category: Large Structures]]
	[[Category: Dai, X H]]		[[Category: Dai, X H]]
	[[Category: Du, Y S]]		[[Category: Du, Y S]]

OCA at 09:06, 18 July 2018

2018-07-18T09:06:32Z

←Older revision		Revision as of 09:06, 18 July 2018
Line 18:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 5tc1" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5tc1" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Virus coat protein\|Virus coat protein]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:20, 8 November 2017

2017-11-08T10:20:46Z

←Older revision		Revision as of 10:20, 8 November 2017
Line 18:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 5tc1" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5tc1" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Virus coat protein\|Virus coat protein]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 16:24, 25 January 2017

2017-01-25T16:24:04Z

←Older revision		Revision as of 16:24, 25 January 2017
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	<StructureSection load='5tc1' size='340' side='right' caption='[[5tc1]], [[Resolution\|resolution]] 3.60Å' scene=''>		<StructureSection load='5tc1' size='340' side='right' caption='[[5tc1]], [[Resolution\|resolution]] 3.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5tc1]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_ms2 Enterobacteria ~~phage ms2] and [http://en.wikipedia.org/wiki/Enterobacterio_phage_ms2 Enterobacterio~~ phage ms2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TC1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TC1 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5tc1]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_ms2 Enterobacteria phage ms2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TC1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TC1 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2ms2\|2ms2]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2ms2\|2ms2]]</td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tc1 OCA], [http://pdbe.org/5tc1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tc1 RCSB], [http://www.ebi.ac.uk/pdbsum/5tc1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tc1 ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tc1 OCA], [http://pdbe.org/5tc1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tc1 RCSB], [http://www.ebi.ac.uk/pdbsum/5tc1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tc1 ProSAT]</span></td></tr>
Line 26:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Enterobacteria phage ms2]]		[[Category: Enterobacteria phage ms2]]
-	[[Category: Enterobacterio phage ms2]]
	[[Category: Dai, X H]]		[[Category: Dai, X H]]
	[[Category: Du, Y S]]		[[Category: Du, Y S]]

OCA at 08:27, 18 January 2017

2017-01-18T08:27:35Z

←Older revision		Revision as of 08:27, 18 January 2017
Line 9:		Line 9:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/CAPSD_BPMS2 CAPSD_BPMS2]] Self-assembles to form the T=3 icosahedral virus shell that protects the viral nucleic acid. Acts as a translational repressor by binding with high specificity to a single stem-loop structure in the genomic RNA that contains the initiation codon of the gene for the viral replicase. Involved in virus assembly through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome.<ref>PMID:16531233</ref> <ref>PMID:18662904</ref> <ref>PMID:26608810</ref> <ref>PMID:8254664</ref> <ref>PMID:9245600</ref> <ref>PMID:9469847</ref> [[http://www.uniprot.org/uniprot/MAT_BPMS2 MAT_BPMS2]] The maturation protein is required for the typical attachment of the phage to the side of the bacterial pili (PubMed:23810697). MP binds to sequences located toward each end of the genome, hence circularizing it (PubMed:26608810). The RNA genome-MP complex is released from the capsid upon host receptor binding (PubMed:23810697). MP enters the cell along with the viral RNA (PubMed:4551992).<ref>PMID:23810697</ref> <ref>PMID:26608810</ref> <ref>PMID:4551992</ref>		[[http://www.uniprot.org/uniprot/CAPSD_BPMS2 CAPSD_BPMS2]] Self-assembles to form the T=3 icosahedral virus shell that protects the viral nucleic acid. Acts as a translational repressor by binding with high specificity to a single stem-loop structure in the genomic RNA that contains the initiation codon of the gene for the viral replicase. Involved in virus assembly through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome.<ref>PMID:16531233</ref> <ref>PMID:18662904</ref> <ref>PMID:26608810</ref> <ref>PMID:8254664</ref> <ref>PMID:9245600</ref> <ref>PMID:9469847</ref> [[http://www.uniprot.org/uniprot/MAT_BPMS2 MAT_BPMS2]] The maturation protein is required for the typical attachment of the phage to the side of the bacterial pili (PubMed:23810697). MP binds to sequences located toward each end of the genome, hence circularizing it (PubMed:26608810). The RNA genome-MP complex is released from the capsid upon host receptor binding (PubMed:23810697). MP enters the cell along with the viral RNA (PubMed:4551992).<ref>PMID:23810697</ref> <ref>PMID:26608810</ref> <ref>PMID:4551992</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Packaging of the genome into a protein capsid and its subsequent delivery into a host cell are two fundamental processes in the life cycle of a virus. Unlike double-stranded DNA viruses, which pump their genome into a preformed capsid, single-stranded RNA (ssRNA) viruses, such as bacteriophage MS2, co-assemble their capsid with the genome; however, the structural basis of this co-assembly is poorly understood. MS2 infects Escherichia coli via the host 'sex pilus' (F-pilus); it was the first fully sequenced organism and is a model system for studies of translational gene regulation, RNA-protein interactions, and RNA virus assembly. Its positive-sense ssRNA genome of 3,569 bases is enclosed in a capsid with one maturation protein monomer and 89 coat protein dimers arranged in a T = 3 icosahedral lattice. The maturation protein is responsible for attaching the virus to an F-pilus and delivering the viral genome into the host during infection, but how the genome is organized and delivered is not known. Here we describe the MS2 structure at 3.6 A resolution, determined by electron-counting cryo-electron microscopy (cryoEM) and asymmetric reconstruction. We traced approximately 80% of the backbone of the viral genome, built atomic models for 16 RNA stem-loops, and identified three conserved motifs of RNA-coat protein interactions among 15 of these stem-loops with diverse sequences. The stem-loop at the 3' end of the genome interacts extensively with the maturation protein, which, with just a six-helix bundle and a six-stranded beta-sheet, forms a genome-delivery apparatus and joins 89 coat protein dimers to form a capsid. This atomic description of genome-capsid interactions in a spherical ssRNA virus provides insight into genome delivery via the host sex pilus and mechanisms underlying ssRNA-capsid co-assembly, and inspires speculation about the links between nucleoprotein complexes and the origins of viruses.
		+
		+	In situ structures of the genome and genome-delivery apparatus in a single-stranded RNA virus.,Dai X, Li Z, Lai M, Shu S, Du Y, Zhou ZH, Sun R Nature. 2017 Jan 5;541(7635):112-116. doi: 10.1038/nature20589. Epub 2016 Dec 19. PMID:27992877<ref>PMID:27992877</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5tc1" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Virus coat protein\|Virus coat protein]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 02:19, 11 December 2016

2016-12-11T02:19:18Z

←Older revision		Revision as of 02:19, 11 December 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5tc1 is ~~ON HOLD until Paper Publication~~	+	==In situ structures of the genome and genome-delivery apparatus in ssRNA bacteriophage MS2==
-		+	<StructureSection load='5tc1' size='340' side='right' caption='[[5tc1]], [[Resolution\|resolution]] 3.60Å' scene=''>
-	~~Authors~~: ~~Dai, X~~.H.~~, Li, Z~~.H., ~~Lai, M~~., ~~Shu, S~~., ~~Du, Y~~.S., ~~Zhou, Z~~.H., ~~Sun, R~~.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5tc1]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_ms2 Enterobacteria phage ms2] and [http://en.wikipedia.org/wiki/Enterobacterio_phage_ms2 Enterobacterio phage ms2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TC1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TC1 FirstGlance]. <br>
-	~~Description~~: ~~In situ structures~~ of the ~~genome~~ and genome-~~delivery apparatus in ssRNA bacteriophage MS2~~	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2ms2\|2ms2]]</td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tc1 OCA], [http://pdbe.org/5tc1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tc1 RCSB], [http://www.ebi.ac.uk/pdbsum/5tc1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tc1 ProSAT]</span></td></tr>
-	[[Category: Dai, X.H]]	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CAPSD_BPMS2 CAPSD_BPMS2]] Self-assembles to form the T=3 icosahedral virus shell that protects the viral nucleic acid. Acts as a translational repressor by binding with high specificity to a single stem-loop structure in the genomic RNA that contains the initiation codon of the gene for the viral replicase. Involved in virus assembly through the interaction between a capsid protein dimer and the multiple packaging signals present in the RNA genome.<ref>PMID:16531233</ref> <ref>PMID:18662904</ref> <ref>PMID:26608810</ref> <ref>PMID:8254664</ref> <ref>PMID:9245600</ref> <ref>PMID:9469847</ref> [[http://www.uniprot.org/uniprot/MAT_BPMS2 MAT_BPMS2]] The maturation protein is required for the typical attachment of the phage to the side of the bacterial pili (PubMed:23810697). MP binds to sequences located toward each end of the genome, hence circularizing it (PubMed:26608810). The RNA genome-MP complex is released from the capsid upon host receptor binding (PubMed:23810697). MP enters the cell along with the viral RNA (PubMed:4551992).<ref>PMID:23810697</ref> <ref>PMID:26608810</ref> <ref>PMID:4551992</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Enterobacteria phage ms2]]
		+	[[Category: Enterobacterio phage ms2]]
		+	[[Category: Dai, X H]]
		+	[[Category: Du, Y S]]
		+	[[Category: Lai, M]]
		+	[[Category: Li, Z H]]
	[[Category: Shu, S]]		[[Category: Shu, S]]
-	[[Category: Lai, M]]
-	[[Category: Zhou, Z.H]]
-	[[Category: Du, Y.S]]
-	[[Category: Li, Z.H]]
	[[Category: Sun, R]]		[[Category: Sun, R]]
		+	[[Category: Zhou, Z H]]
		+	[[Category: Asymmetric cryoem reconstruction]]
		+	[[Category: Genome-capsid interaction]]
		+	[[Category: Genome-delivery apparatus]]
		+	[[Category: Ssrna genome structure]]
		+	[[Category: Viral protein-rna complex]]

OCA at 15:38, 19 October 2016

2016-10-19T15:38:17Z

←Older revision		Revision as of 15:38, 19 October 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5tc1 is ON HOLD	+	The entry 5tc1 is ON HOLD until Paper Publication

	Authors: Dai, X.H., Li, Z.H., Lai, M., Shu, S., Du, Y.S., Zhou, Z.H., Sun, R.		Authors: Dai, X.H., Li, Z.H., Lai, M., Shu, S., Du, Y.S., Zhou, Z.H., Sun, R.

OCA: Protected "5tc1" [edit=sysop:move=sysop]

2016-09-21T12:29:09Z

Protected "5tc1" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:29, 21 September 2016