3j22 - Revision history

OCA at 10:09, 21 February 2024

OCA — Wed, 21 Feb 2024 10:09:38 GMT

←Older revision		Revision as of 10:09, 21 February 2024
Line 9:		Line 9:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/B2ZUN0_HE71 B2ZUN0_HE71] 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. After genome has been released, the channel shrinks.[RuleBase:RU364118] Protease 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins.[RuleBase:RU364118] Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1.[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 dissassembly 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: Is 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. The 3C domain in the context of protein 3CD may have an RNA binding activity.[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. VPg may be removed in the cytoplasm by an unknown enzyme termed "unlinkase". VPg is not cleaved off virion genomes because replicated genomic RNA are encapsidated at the site of replication.[RuleBase:RU364118]		[https://www.uniprot.org/uniprot/B2ZUN0_HE71 B2ZUN0_HE71] 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. After genome has been released, the channel shrinks.[RuleBase:RU364118] Protease 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins.[RuleBase:RU364118] Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1.[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 dissassembly 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: Is 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. The 3C domain in the context of protein 3CD may have an RNA binding activity.[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. VPg may be removed in the cytoplasm by an unknown enzyme termed "unlinkase". VPg is not cleaved off virion genomes because replicated genomic RNA are encapsidated at the site of replication.[RuleBase:RU364118]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Since its discovery in 1969, enterovirus 71 (EV71) has emerged as a serious worldwide health threat. This human pathogen of the picornavirus family causes hand, foot, and mouth disease, and also has the capacity to invade the central nervous system to cause severe disease and death. Upon binding to a host receptor on the cell surface, the virus begins a two-step uncoating process, first forming an expanded, altered "A-particle", which is primed for genome release. In a second step after endocytosis, an unknown trigger leads to RNA expulsion, generating an intact, empty capsid. Cryo-electron microscopy reconstructions of these two capsid states provide insight into the mechanics of genome release. The EV71 A-particle capsid interacts with the genome near the icosahedral two-fold axis of symmetry, which opens to the external environment via a channel approximately 10 A in diameter that is lined with patches of negatively charged residues. After the EV71 genome has been released, the two-fold channel shrinks, though the overall capsid dimensions are conserved. These structural characteristics identify the two-fold channel as the site where a gateway forms and regulates the process of genome release.
-
-	The Enterovirus 71 A-particle Forms a Gateway to Allow Genome Release: A CryoEM Study of Picornavirus Uncoating.,Shingler KL, Yoder JL, Carnegie MS, Ashley RE, Makhov AM, Conway JF, Hafenstein S PLoS Pathog. 2013 Mar;9(3):e1003240. doi: 10.1371/journal.ppat.1003240. Epub 2013, Mar 21. PMID:23555253<ref>PMID:23555253</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 3j22" style="background-color:#fffaf0;"></div>

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

OCA at 14:13, 24 January 2024

OCA — Wed, 24 Jan 2024 14:13:42 GMT

←Older revision		Revision as of 14:13, 24 January 2024
Line 3:		Line 3:
	<SX load='3j22' size='340' side='right' viewer='molstar' caption='[[3j22]], [[Resolution\|resolution]] 6.30Å' scene=''>		<SX load='3j22' size='340' side='right' viewer='molstar' caption='[[3j22]], [[Resolution\|resolution]] 6.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3j22]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human_enterovirus_71 Human enterovirus 71~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J22 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J22 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3j22]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterovirus_A71 Enterovirus A71]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J22 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J22 FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style~~=~~'overflow: auto; max-height: 3em;'~~>[[~~3j23~~\|~~3j23~~]]~~</div>~~</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]] 6.3Å</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=3j22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j22 OCA], [https://pdbe.org/3j22 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j22 RCSB], [https://www.ebi.ac.uk/pdbsum/3j22 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j22 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=3j22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j22 OCA], [https://pdbe.org/3j22 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j22 RCSB], [https://www.ebi.ac.uk/pdbsum/3j22 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j22 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/~~B2ZUN0_9ENTO B2ZUN0_9ENTO~~]] Protein 2C associates with ~~and induces~~ structural rearrangements of intracellular membranes. ~~It displays~~ RNA-binding, nucleotide binding and NTPase activities ~~(By similarity)~~.[~~SAAS~~:~~SAAS000199_004_016611~~] Protein ~~3C is a cysteine protease that generates mature~~ viral ~~proteins from~~ the ~~precursor polyprotein~~. ~~In addition~~ to ~~its proteolytic activity~~, ~~it binds to viral RNA~~, and ~~thus influences~~ viral ~~genome~~ replication. ~~RNA and substrate bind co~~-~~operatively~~ to the protease ~~(By similarity)~~.[~~SAAS~~:~~SAAS000199_004_042266~~] RNA-directed RNA polymerase 3D-~~POL replicates~~ genomic and ~~antigenomic~~ RNA ~~by recognizing replications specific signals~~ (~~By similarity~~).[~~SAAS~~:~~SAAS000199_004_010047~~]	+	[https://www.uniprot.org/uniprot/B2ZUN0_HE71 B2ZUN0_HE71] 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. After genome has been released, the channel shrinks.[RuleBase:RU364118] Protease 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins.[RuleBase:RU364118] Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1.[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 dissassembly 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: Is 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. The 3C domain in the context of protein 3CD may have an RNA binding activity.[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. VPg may be removed in the cytoplasm by an unknown enzyme termed "unlinkase". VPg is not cleaved off virion genomes because replicated genomic RNA are encapsidated at the site of replication.[RuleBase:RU364118]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 25:
	__TOC__		__TOC__
	</SX>		</SX>
-	[[Category: ~~Human enterovirus 71~~]]	+	[[Category: Enterovirus A71]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Shingler~~, K L]]~~	+	[[Category: Shingler KL]]
-	~~[[Category: Ev71]]~~	+
-	~~[[Category: Virus~~]]	+

OCA at 03:48, 21 April 2022

OCA — Thu, 21 Apr 2022 03:48:06 GMT

←Older revision		Revision as of 03:48, 21 April 2022
Line 3:		Line 3:
	<SX load='3j22' size='340' side='right' viewer='molstar' caption='[[3j22]], [[Resolution\|resolution]] 6.30Å' scene=''>		<SX load='3j22' size='340' side='right' viewer='molstar' caption='[[3j22]], [[Resolution\|resolution]] 6.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3j22]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human_enterovirus_71 Human enterovirus 71]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J22 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=3J22 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3j22]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_enterovirus_71 Human enterovirus 71]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J22 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J22 FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3j23\|3j23]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3j23\|3j23]]</div></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=3j22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j22 OCA], [~~http~~://pdbe.org/3j22 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3j22 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3j22 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3j22 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=3j22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j22 OCA], [https://pdbe.org/3j22 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j22 RCSB], [https://www.ebi.ac.uk/pdbsum/3j22 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j22 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/B2ZUN0_9ENTO B2ZUN0_9ENTO]] Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).[SAAS:SAAS000199_004_016611] Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity).[SAAS:SAAS000199_004_042266] RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).[SAAS:SAAS000199_004_010047]	+	[[https://www.uniprot.org/uniprot/B2ZUN0_9ENTO B2ZUN0_9ENTO]] Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).[SAAS:SAAS000199_004_016611] Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity).[SAAS:SAAS000199_004_042266] RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).[SAAS:SAAS000199_004_010047]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 18:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 3j22" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3j22" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Virus coat proteins 3D structures\|Virus coat proteins 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 17:44, 10 April 2020

OCA — Fri, 10 Apr 2020 17:44:37 GMT

←Older revision		Revision as of 17:44, 10 April 2020
Line 3:		Line 3:
	<SX load='3j22' size='340' side='right' viewer='molstar' caption='[[3j22]], [[Resolution\|resolution]] 6.30Å' scene=''>		<SX load='3j22' size='340' side='right' viewer='molstar' caption='[[3j22]], [[Resolution\|resolution]] 6.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3j22]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_enterovirus_71 Human enterovirus 71]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J22 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3J22 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3j22]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_enterovirus_71 Human enterovirus 71]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J22 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3J22 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3j23\|3j23]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3j23\|3j23]]</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=3j22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j22 OCA], [http://pdbe.org/3j22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j22 RCSB], [http://www.ebi.ac.uk/pdbsum/3j22 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j22 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=3j22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j22 OCA], [http://pdbe.org/3j22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j22 RCSB], [http://www.ebi.ac.uk/pdbsum/3j22 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j22 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 17:18, 6 March 2020

OCA — Fri, 06 Mar 2020 17:18:13 GMT

←Older revision		Revision as of 17:18, 6 March 2020
Line 1:		Line 1:

	==The Enterovirus 71 A-particle==		==The Enterovirus 71 A-particle==
-	<~~StructureSection~~ load='3j22' size='340' side='right' caption='[[3j22]], [[Resolution\|resolution]] 6.30Å' scene=''>	+	<SX load='3j22' size='340' side='right' viewer='molstar' caption='[[3j22]], [[Resolution\|resolution]] 6.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3j22]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_enterovirus_71 Human enterovirus 71]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J22 FirstGlance]. <br>		<table><tr><td colspan='2'>[[3j22]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_enterovirus_71 Human enterovirus 71]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J22 FirstGlance]. <br>
Line 21:		Line 21:
	<references/>		<references/>
	__TOC__		__TOC__
-	</~~StructureSection~~>	+	</SX>
	[[Category: Human enterovirus 71]]		[[Category: Human enterovirus 71]]
		+	[[Category: Large Structures]]
	[[Category: Shingler, K L]]		[[Category: Shingler, K L]]
	[[Category: Ev71]]		[[Category: Ev71]]
	[[Category: Virus]]		[[Category: Virus]]

OCA at 08:07, 18 July 2018

OCA — Wed, 18 Jul 2018 08:07:48 GMT

←Older revision		Revision as of 08:07, 18 July 2018
Line 3:		Line 3:
	<StructureSection load='3j22' size='340' side='right' caption='[[3j22]], [[Resolution\|resolution]] 6.30Å' scene=''>		<StructureSection load='3j22' size='340' side='right' caption='[[3j22]], [[Resolution\|resolution]] 6.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3j22]] 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=3J22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J22 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3j22]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_enterovirus_71 Human enterovirus 71]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J22 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3j23\|3j23]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3j23\|3j23]]</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=3j22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j22 OCA], [http://pdbe.org/3j22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j22 RCSB], [http://www.ebi.ac.uk/pdbsum/3j22 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j22 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=3j22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j22 OCA], [http://pdbe.org/3j22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j22 RCSB], [http://www.ebi.ac.uk/pdbsum/3j22 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j22 ProSAT]</span></td></tr>
Line 22:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Ev-~~71]]	+	[[Category: Human enterovirus 71]]
	[[Category: Shingler, K L]]		[[Category: Shingler, K L]]
	[[Category: Ev71]]		[[Category: Ev71]]
	[[Category: Virus]]		[[Category: Virus]]

OCA at 10:06, 4 August 2016

OCA — Thu, 04 Aug 2016 10:06:47 GMT

←Older revision		Revision as of 10:06, 4 August 2016
Line 1:		Line 1:
		+
	==The Enterovirus 71 A-particle==		==The Enterovirus 71 A-particle==
	<StructureSection load='3j22' size='340' side='right' caption='[[3j22]], [[Resolution\|resolution]] 6.30Å' scene=''>		<StructureSection load='3j22' size='340' side='right' caption='[[3j22]], [[Resolution\|resolution]] 6.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3j22]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Ev-71 Ev-71~~] and [http://en.wikipedia.org/wiki/Gekko_coi Gekko coi~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J22 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3j22]] 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=3J22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J22 FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3j23\|3j23]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3j23\|3j23]]</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=3j22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j22 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j22 RCSB], [http://www.ebi.ac.uk/pdbsum/3j22 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=3j22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j22 OCA], [http://pdbe.org/3j22 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j22 RCSB], [http://www.ebi.ac.uk/pdbsum/3j22 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j22 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 17:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3j22" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 21:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Ev-71]]		[[Category: Ev-71]]
-	[[Category: Gekko coi]]
	[[Category: Shingler, K L]]		[[Category: Shingler, K L]]
	[[Category: Ev71]]		[[Category: Ev71]]
	[[Category: Virus]]		[[Category: Virus]]

OCA at 08:43, 24 December 2014

OCA — Wed, 24 Dec 2014 08:43:08 GMT

←Older revision		Revision as of 08:43, 24 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3j22\| PDB~~=3j22 \| ~~SCENE~~= }}	+	==The Enterovirus 71 A-particle==
-	===~~The Enterovirus~~ 71 A-~~particle~~===	+	<StructureSection load='3j22' size='340' side='right' caption='[[3j22]], [[Resolution\|resolution]] 6.30Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23555253}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[3j22]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Ev-71 Ev-71] and [http://en.wikipedia.org/wiki/Gekko_coi Gekko coi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J22 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J22 FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3j23\|3j23]]</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=3j22 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j22 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j22 RCSB], [http://www.ebi.ac.uk/pdbsum/3j22 PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/B2ZUN0_9ENTO B2ZUN0_9ENTO]] Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).[SAAS:SAAS000199_004_016611] Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity).[SAAS:SAAS000199_004_042266] RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).[SAAS:SAAS000199_004_010047]		[[http://www.uniprot.org/uniprot/B2ZUN0_9ENTO B2ZUN0_9ENTO]] Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).[SAAS:SAAS000199_004_016611] Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity).[SAAS:SAAS000199_004_042266] RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).[SAAS:SAAS000199_004_010047]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Since its discovery in 1969, enterovirus 71 (EV71) has emerged as a serious worldwide health threat. This human pathogen of the picornavirus family causes hand, foot, and mouth disease, and also has the capacity to invade the central nervous system to cause severe disease and death. Upon binding to a host receptor on the cell surface, the virus begins a two-step uncoating process, first forming an expanded, altered "A-particle", which is primed for genome release. In a second step after endocytosis, an unknown trigger leads to RNA expulsion, generating an intact, empty capsid. Cryo-electron microscopy reconstructions of these two capsid states provide insight into the mechanics of genome release. The EV71 A-particle capsid interacts with the genome near the icosahedral two-fold axis of symmetry, which opens to the external environment via a channel approximately 10 A in diameter that is lined with patches of negatively charged residues. After the EV71 genome has been released, the two-fold channel shrinks, though the overall capsid dimensions are conserved. These structural characteristics identify the two-fold channel as the site where a gateway forms and regulates the process of genome release.
		+
		+	The Enterovirus 71 A-particle Forms a Gateway to Allow Genome Release: A CryoEM Study of Picornavirus Uncoating.,Shingler KL, Yoder JL, Carnegie MS, Ashley RE, Makhov AM, Conway JF, Hafenstein S PLoS Pathog. 2013 Mar;9(3):e1003240. doi: 10.1371/journal.ppat.1003240. Epub 2013, Mar 21. PMID:23555253<ref>PMID:23555253</ref>

-	==~~About this Structure~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[3j22]] is a 3 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Gekko_coi Gekko coi] and~~ [~~http://en.wikipedia.org/wiki/Human_enterovirus_71 Human enterovirus 71]. Full crystallographic information is available from~~ [~~http~~:~~//oca.weizmann.ac.il/oca~~-~~bin/ocashort?id=3J22 OCA~~].	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Ev-71]]
	[[Category: Gekko coi]]		[[Category: Gekko coi]]
-	~~[[Category: Human enterovirus 71]]~~	+	[[Category: Shingler, K L]]
-	[[Category: Shingler, K L~~.]]~~	+
-	~~[[Category: 135~~]]	+
	[[Category: Ev71]]		[[Category: Ev71]]
	[[Category: Virus]]		[[Category: Virus]]

OCA at 19:22, 17 April 2013

OCA — Wed, 17 Apr 2013 19:22:27 GMT

←Older revision		Revision as of 19:22, 17 April 2013
Line 1:		Line 1:
	{{STRUCTURE_3j22\| PDB=3j22 \| SCENE= }}		{{STRUCTURE_3j22\| PDB=3j22 \| SCENE= }}
	===The Enterovirus 71 A-particle===		===The Enterovirus 71 A-particle===
		+	{{ABSTRACT_PUBMED_23555253}}

	==Function==		==Function==

OCA at 01:38, 4 April 2013

OCA — Thu, 04 Apr 2013 01:38:42 GMT

←Older revision		Revision as of 01:38, 4 April 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_3j22\| PDB=3j22 \| SCENE= }}
		+	===The Enterovirus 71 A-particle===

-	~~The entry 3j22~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/B2ZUN0_9ENTO B2ZUN0_9ENTO]] Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).[SAAS:SAAS000199_004_016611] Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease (By similarity).[SAAS:SAAS000199_004_042266] RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals (By similarity).[SAAS:SAAS000199_004_010047]

-	~~Authors~~: Shingler, K.S.	+	==About this Structure==
-		+	[[3j22]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Gekko_coi Gekko coi] and [http://en.wikipedia.org/wiki/Human_enterovirus_71 Human enterovirus 71]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J22 OCA].
-	~~Description~~: ~~The Enterovirus 71 A-particle~~	+	[[Category: Gekko coi]]
		+	[[Category: Human enterovirus 71]]
		+	[[Category: Shingler, K L.]]
		+	[[Category: 135]]
		+	[[Category: Ev71]]
		+	[[Category: Virus]]