6qjt - Revision history

OCA at 15:25, 8 June 2021

OCA — Tue, 08 Jun 2021 15:25:35 GMT

←Older revision		Revision as of 15:25, 8 June 2021
Line 3:		Line 3:
	<StructureSection load='6qjt' size='340' side='right'caption='[[6qjt]], [[Resolution\|resolution]] 3.74Å' scene=''>		<StructureSection load='6qjt' size='340' side='right'caption='[[6qjt]], [[Resolution\|resolution]] 3.74Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6qjt]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Thermus_virus_p23-45 Thermus virus p23-45]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QJT OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6QJT FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6qjt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_virus_p23-45 Thermus virus p23-45]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QJT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QJT FirstGlance]. <br>
-	</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=6qjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qjt OCA], [~~http~~://pdbe.org/6qjt PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6qjt RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6qjt PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6qjt ProSAT]</span></td></tr>	+	</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=6qjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qjt OCA], [https://pdbe.org/6qjt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qjt RCSB], [https://www.ebi.ac.uk/pdbsum/6qjt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qjt ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PORTL_BP234 PORTL_BP234]] Forms the portal vertex of the capsid (By similarity). This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection (By similarity). The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel (By similarity). Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection (By similarity).[UniProtKB:A0A1L4BKQ4]	+	[[https://www.uniprot.org/uniprot/PORTL_BP234 PORTL_BP234]] Forms the portal vertex of the capsid (By similarity). This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection (By similarity). The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel (By similarity). Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection (By similarity).[UniProtKB:A0A1L4BKQ4]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</div>		</div>
	<div class="pdbe-citations 6qjt" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6qjt" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Portal protein\|Portal protein]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:04, 22 April 2020

OCA — Wed, 22 Apr 2020 06:04:37 GMT

←Older revision		Revision as of 06:04, 22 April 2020
Line 3:		Line 3:
	<StructureSection load='6qjt' size='340' side='right'caption='[[6qjt]], [[Resolution\|resolution]] 3.74Å' scene=''>		<StructureSection load='6qjt' size='340' side='right'caption='[[6qjt]], [[Resolution\|resolution]] 3.74Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6qjt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_virus_p23-45 Thermus virus p23-45]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QJT OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6QJT FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6qjt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_virus_p23-45 Thermus virus p23-45]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QJT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6QJT FirstGlance]. <br>
-	</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=6qjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qjt OCA], [http://pdbe.org/6qjt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qjt RCSB], [http://www.ebi.ac.uk/pdbsum/6qjt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qjt ProSAT]</span></td></tr>	+	</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=6qjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qjt OCA], [http://pdbe.org/6qjt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qjt RCSB], [http://www.ebi.ac.uk/pdbsum/6qjt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qjt ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/PORTL_BP234 PORTL_BP234]] Forms the portal vertex of the capsid (By similarity). This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection (By similarity). The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel (By similarity). Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection (By similarity).[UniProtKB:A0A1L4BKQ4]		[[http://www.uniprot.org/uniprot/PORTL_BP234 PORTL_BP234]] Forms the portal vertex of the capsid (By similarity). This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection (By similarity). The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel (By similarity). Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection (By similarity).[UniProtKB:A0A1L4BKQ4]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The portal protein is a key component of many double-stranded DNA viruses, governing capsid assembly and genome packaging. Twelve subunits of the portal protein define a tunnel, through which DNA is translocated into the capsid. It is unknown how the portal protein functions as a gatekeeper, preventing DNA slippage, whilst allowing its passage into the capsid, and how these processes are controlled. A cryo-EM structure of the portal protein of thermostable virus P23-45, determined in situ in its procapsid-bound state, indicates a mechanism that naturally safeguards the virus against genome loss. This occurs via an inversion of the conformation of the loops that define the constriction in the central tunnel, accompanied by a hydrophilic-hydrophobic switch. The structure also shows how translocation of DNA into the capsid could be modulated by a changing mode of protein-protein interactions between portal and capsid, across a symmetry-mismatched interface.
		+
		+	Cryo-EM structure in situ reveals a molecular switch that safeguards virus against genome loss.,Bayfield OW, Steven AC, Antson AA Elife. 2020 Apr 14;9. pii: 55517. doi: 10.7554/eLife.55517. PMID:32286226<ref>PMID:32286226</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6qjt" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 10:14, 27 March 2020

OCA — Fri, 27 Mar 2020 10:14:25 GMT

←Older revision		Revision as of 10:14, 27 March 2020
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-	'''Unreleased structure'''

-	~~The entry~~ 6qjt ~~is ON HOLD~~	+	==Thermophage P23-45 in situ procapsid portal protein==
-		+	<StructureSection load='6qjt' size='340' side='right'caption='[[6qjt]], [[Resolution\|resolution]] 3.74Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6qjt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_virus_p23-45 Thermus virus p23-45]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QJT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QJT FirstGlance]. <br>
-	~~Description~~:	+	</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=6qjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qjt OCA], [http://pdbe.org/6qjt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qjt RCSB], [http://www.ebi.ac.uk/pdbsum/6qjt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qjt ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PORTL_BP234 PORTL_BP234]] Forms the portal vertex of the capsid (By similarity). This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection (By similarity). The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel (By similarity). Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection (By similarity).[UniProtKB:A0A1L4BKQ4]
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Thermus virus p23-45]]
		+	[[Category: Antson, A A]]
		+	[[Category: Bayfield, O W]]
		+	[[Category: Bacteriophage]]
		+	[[Category: Caudovirale]]
		+	[[Category: Motor]]
		+	[[Category: Pore]]
		+	[[Category: Portal]]
		+	[[Category: Siphoviridae]]
		+	[[Category: Thermophage]]
		+	[[Category: Translocase]]
		+	[[Category: Viral protein]]
		+	[[Category: Virus]]

OCA: Protected "6qjt" [edit=sysop:move=sysop]

OCA — Wed, 30 Jan 2019 07:04:45 GMT

Protected "6qjt" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:04, 30 January 2019

OCA: New page: '''Unreleased structure''' The entry 6qjt is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 30 Jan 2019 07:04:43 GMT

New page: '''Unreleased structure''' The entry 6qjt is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6qjt is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]