5f8l - Revision history

OCA at 06:42, 19 July 2023

2023-07-19T06:42:11Z

←Older revision		Revision as of 06:42, 19 July 2023
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	<StructureSection load='5f8l' size='340' side='right'caption='[[5f8l]], [[Resolution\|resolution]] 2.81Å' scene=''>		<StructureSection load='5f8l' size='340' side='right'caption='[[5f8l]], [[Resolution\|resolution]] 2.81Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5f8l]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Ev-71 Ev-71~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F8L OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5F8L FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5f8l]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterovirus_A71 Enterovirus A71] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F8L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F8L FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.812Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~>[[5f8g\|5f8g]], [[5f8h\|5f8h]], [[5f8i\|5f8i]], [[5f8j\|5f8j]], [[5f8m\|5f8m]], [[5f8n\|5f8n]], [[5f8o\|5f8o]]</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr~~ id~~='activity'><td class~~="~~sblockLbl~~"><~~b>Activity:</b></td><td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48]~~ </~~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=5f8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f8l OCA], [https://pdbe.org/5f8l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f8l RCSB], [https://www.ebi.ac.uk/pdbsum/5f8l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f8l 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=5f8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f8l OCA], [~~http~~://pdbe.org/5f8l PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5f8l RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5f8l PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5f8l ProSAT]</span></td></tr>	+
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/E5RPG2_HE71 E5RPG2_HE71] Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU (By similarity). The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome (By similarity). Following genome release from the infecting virion in the cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (By similarity). During the late stage of the replication cycle, host TDP2 is excluded from sites of viral RNA synthesis and encapsidation, allowing for the generation of progeny virions.[ARBA:ARBA00024846] Capsid protein VP0: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step.[RuleBase:RU364118] Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host cell receptor to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks.[RuleBase:RU364118] Capsid protein VP2: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome.[RuleBase:RU364118] Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome.[RuleBase:RU364118] Capsid protein VP4: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm.[RuleBase:RU364118] Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation (By similarity). Allows the capsid to remain inactive before the maturation step.[ARBA:ARBA00025202] Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome.[ARBA:ARBA00025306] Lies on the inner surface of the capsid shell (By similarity). After binding to the host receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm.[ARBA:ARBA00024643] Protease 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins.[RuleBase:RU364118] Protease 3C: Major viral protease that mediates proteolytic processing of the polyprotein. Cleaves host EIF5B, contributing to host translation shutoff. Cleaves also host PABPC1, contributing to host translation shutoff.[RuleBase:RU364118] Protein 2B: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication.[RuleBase:RU364118] Protein 2C: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3.[RuleBase:RU364118] Protein 3A: Localizes the viral replication complex to the surface of membranous vesicles. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the disassembly of the Golgi complex, possibly through GBF1 interaction. This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface.[RuleBase:RU364118] Protein 3AB: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity.[RuleBase:RU364118] Protein 3CD: Involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. Protein 3CD binds to the 5'UTR of the viral genome.[RuleBase:RU364118] RNA-directed RNA polymerase: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss(+)RNA genomes are either translated, replicated or encapsidated.[RuleBase:RU364118] Viral protein genome-linked: acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome.[RuleBase:RU364118]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Ev-71~~]]	+	[[Category: Enterovirus A71]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~RNA-directed RNA polymerase~~]]	+	[[Category: Synthetic construct]]
-	[[Category: Gong, P]]	+	[[Category: Gong P]]
-	[[Category: Shu, B]]	+	[[Category: Shu B]]
-	~~[[Category: Elongation]]~~	+
-	~~[[Category: Nucleotide addition cycle]]~~	+
-	~~[[Category: Polymerase-rna complex]]~~	+
-	~~[[Category: Transferase-rna complex~~]]	+

OCA at 08:04, 29 April 2020

2020-04-29T08:04:38Z

←Older revision		Revision as of 08:04, 29 April 2020
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	==Enterovirus 71 Polymerase Elongation Complex (C3S1 Form)==		==Enterovirus 71 Polymerase Elongation Complex (C3S1 Form)==
-	<StructureSection load='5f8l' size='340' side='right' caption='[[5f8l]], [[Resolution\|resolution]] 2.81Å' scene=''>	+	<StructureSection load='5f8l' size='340' side='right'caption='[[5f8l]], [[Resolution\|resolution]] 2.81Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5f8l]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F8L OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5F8L FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5f8l]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Ev-71 Ev-71]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F8L OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5F8L FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5f8g\|5f8g]], [[5f8h\|5f8h]], [[5f8i\|5f8i]], [[5f8j\|5f8j]], [[5f8m\|5f8m]], [[5f8n\|5f8n]], [[5f8o\|5f8o]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5f8g\|5f8g]], [[5f8h\|5f8h]], [[5f8i\|5f8i]], [[5f8j\|5f8j]], [[5f8m\|5f8m]], [[5f8n\|5f8n]], [[5f8o\|5f8o]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] </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=5f8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f8l OCA], [http://pdbe.org/5f8l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f8l RCSB], [http://www.ebi.ac.uk/pdbsum/5f8l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f8l 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=5f8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f8l OCA], [http://pdbe.org/5f8l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f8l RCSB], [http://www.ebi.ac.uk/pdbsum/5f8l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f8l ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Ev-71]]
		+	[[Category: Large Structures]]
	[[Category: RNA-directed RNA polymerase]]		[[Category: RNA-directed RNA polymerase]]
	[[Category: Gong, P]]		[[Category: Gong, P]]

OCA at 20:43, 3 August 2016

2016-08-03T20:43:02Z

←Older revision		Revision as of 20:43, 3 August 2016
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	<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=5f8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f8l OCA], [http://pdbe.org/5f8l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f8l RCSB], [http://www.ebi.ac.uk/pdbsum/5f8l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f8l 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=5f8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f8l OCA], [http://pdbe.org/5f8l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f8l RCSB], [http://www.ebi.ac.uk/pdbsum/5f8l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f8l ProSAT]</span></td></tr>
	</table>		</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Viral RNA-dependent RNA polymerases (RdRPs) play essential roles in viral genome replication and transcription. We previously reported several structural states of the poliovirus RdRP nucleotide addition cycle (NAC) that revealed a unique palm domain-based active site closure mechanism and proposed a six-state NAC model including a hypothetical state representing translocation intermediates. Using the RdRP from another human enterovirus, enterovirus 71, here we report seven RdRP elongation complex structures derived from a crystal lattice that allows three NAC events. These structures suggested a key order of events in initial NTP binding and NTP-induced active site closure and revealed a bona fide translocation intermediate featuring asymmetric movement of the template-product duplex. Our work provides essential missing links in understanding NTP recognition and translocation mechanisms in viral RdRPs and emphasizes the uniqueness of the viral RdRPs compared with other processive polymerases.
		+
		+	Structural basis of viral RNA-dependent RNA polymerase catalysis and translocation.,Shu B, Gong P Proc Natl Acad Sci U S A. 2016 Jul 12;113(28):E4005-14. doi:, 10.1073/pnas.1602591113. Epub 2016 Jun 23. PMID:27339134<ref>PMID:27339134</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5f8l" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 02:25, 13 July 2016

2016-07-13T02:25:32Z

←Older revision		Revision as of 02:25, 13 July 2016
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	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5f8g\|5f8g]], [[5f8h\|5f8h]], [[5f8i\|5f8i]], [[5f8j\|5f8j]], [[5f8m\|5f8m]], [[5f8n\|5f8n]], [[5f8o\|5f8o]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5f8g\|5f8g]], [[5f8h\|5f8h]], [[5f8i\|5f8i]], [[5f8j\|5f8j]], [[5f8m\|5f8m]], [[5f8n\|5f8n]], [[5f8o\|5f8o]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] </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=5f8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f8l OCA], [http://pdbe.org/5f8l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f8l RCSB], [http://www.ebi.ac.uk/pdbsum/5f8l PDBsum]</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=5f8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f8l OCA], [http://pdbe.org/5f8l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f8l RCSB], [http://www.ebi.ac.uk/pdbsum/5f8l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f8l ProSAT]</span></td></tr>
	</table>		</table>
	__TOC__		__TOC__

OCA at 23:25, 23 June 2016

2016-06-23T23:25:31Z

←Older revision		Revision as of 23:25, 23 June 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5f8l is ~~ON HOLD until Paper Publication~~	+	==Enterovirus 71 Polymerase Elongation Complex (C3S1 Form)==
-		+	<StructureSection load='5f8l' size='340' side='right' caption='[[5f8l]], [[Resolution\|resolution]] 2.81Å' scene=''>
-	~~Authors~~: ~~Shu~~, B., ~~Gong~~, P.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5f8l]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F8L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F8L FirstGlance]. <br>
-	~~Description: Enterovirus 71 Polymerase Elongation Complex (C3S1 Form)~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5f8g\|5f8g]], [[5f8h\|5f8h]], [[5f8i\|5f8i]], [[5f8j\|5f8j]], [[5f8m\|5f8m]], [[5f8n\|5f8n]], [[5f8o\|5f8o]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] </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=5f8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f8l OCA], [http://pdbe.org/5f8l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f8l RCSB], [http://www.ebi.ac.uk/pdbsum/5f8l PDBsum]</span></td></tr>
		+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: RNA-directed RNA polymerase]]
	[[Category: Gong, P]]		[[Category: Gong, P]]
	[[Category: Shu, B]]		[[Category: Shu, B]]
		+	[[Category: Elongation]]
		+	[[Category: Nucleotide addition cycle]]
		+	[[Category: Polymerase-rna complex]]
		+	[[Category: Transferase-rna complex]]

OCA at 17:38, 30 December 2015

2015-12-30T17:38:51Z

←Older revision		Revision as of 17:38, 30 December 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5f8l is ON HOLD	+	The entry 5f8l is ON HOLD until Paper Publication

-	Authors: Shu, ~~B., Peersen, O.~~B., Gong, P.	+	Authors: Shu, B., Gong, P.

	Description: Enterovirus 71 Polymerase Elongation Complex (C3S1 Form)		Description: Enterovirus 71 Polymerase Elongation Complex (C3S1 Form)
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	[[Category: Gong, P]]		[[Category: Gong, P]]
-	[[Category: Peersen, O.B]]
	[[Category: Shu, B]]		[[Category: Shu, B]]

OCA: Protected "5f8l" [edit=sysop:move=sysop]

2015-12-16T12:43:31Z

Protected "5f8l" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:43, 16 December 2015

OCA: New page: '''Unreleased structure''' The entry 5f8l is ON HOLD Authors: Shu, B., Peersen, O.B., Gong, P. Description: Enterovirus 71 Polymerase Elongation Complex (C3S1 Form) [[Category: Unrelea...

2015-12-16T12:43:30Z

New page: '''Unreleased structure''' The entry 5f8l is ON HOLD Authors: Shu, B., Peersen, O.B., Gong, P. Description: Enterovirus 71 Polymerase Elongation Complex (C3S1 Form) [[Category: Unrelea...

New page

'''Unreleased structure'''

The entry 5f8l is ON HOLD

Authors: Shu, B., Peersen, O.B., Gong, P.

Description: Enterovirus 71 Polymerase Elongation Complex (C3S1 Form)
[[Category: Unreleased Structures]]
[[Category: Gong, P]]
[[Category: Peersen, O.B]]
[[Category: Shu, B]]