4n0n - Revision history

OCA at 12:30, 1 March 2024

OCA — Fri, 01 Mar 2024 12:30:36 GMT

←Older revision		Revision as of 12:30, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4n0n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equine_arteritis_virus_Bucyrus Equine arteritis virus Bucyrus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N0N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N0N FirstGlance]. <br>		<table><tr><td colspan='2'>[[4n0n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equine_arteritis_virus_Bucyrus Equine arteritis virus Bucyrus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N0N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N0N FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <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]] 2Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4n0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n0n OCA], [https://pdbe.org/4n0n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n0n RCSB], [https://www.ebi.ac.uk/pdbsum/4n0n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n0n 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=4n0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n0n OCA], [https://pdbe.org/4n0n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n0n RCSB], [https://www.ebi.ac.uk/pdbsum/4n0n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n0n ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/RPOA_EAVBU RPOA_EAVBU] The replicase polyprotein 1ab is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.<ref>PMID:18078692</ref> Nsp1 is essential for viral subgenomic mRNA synthesis.<ref>PMID:18078692</ref> Nsp2 cysteine proteinase which cleaves the nsp2/nsp3 site in the polyprotein. Also displays deubiquitinating and deISGylase activities. The deubiquitinating activity cleaves both ubiquitinated and ISGylated products and may therefore regulate ubiquitin and ISG15 dependent host innate immunity.<ref>PMID:18078692</ref> The 3C-like serine proteinase chain is responsible for the majority of cleavages as it cleaves the C-terminus of the polyprotein.<ref>PMID:18078692</ref> The helicase chain, which contains a zinc finger structure, displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity.<ref>PMID:18078692</ref>		[https://www.uniprot.org/uniprot/RPOA_EAVBU RPOA_EAVBU] The replicase polyprotein 1ab is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.<ref>PMID:18078692</ref> Nsp1 is essential for viral subgenomic mRNA synthesis.<ref>PMID:18078692</ref> Nsp2 cysteine proteinase which cleaves the nsp2/nsp3 site in the polyprotein. Also displays deubiquitinating and deISGylase activities. The deubiquitinating activity cleaves both ubiquitinated and ISGylated products and may therefore regulate ubiquitin and ISG15 dependent host innate immunity.<ref>PMID:18078692</ref> The 3C-like serine proteinase chain is responsible for the majority of cleavages as it cleaves the C-terminus of the polyprotein.<ref>PMID:18078692</ref> The helicase chain, which contains a zinc finger structure, displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity.<ref>PMID:18078692</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	All positive-stranded RNA viruses with genomes > approximately 7 kb encode helicases, which generally are poorly characterized. The core of the nidovirus superfamily 1 helicase (HEL1) is associated with a unique N-terminal zinc-binding domain (ZBD) that was previously implicated in helicase regulation, genome replication and subgenomic mRNA synthesis. The high-resolution structure of the arterivirus helicase (nsp10), alone and in complex with a polynucleotide substrate, now provides first insights into the structural basis for nidovirus helicase function. A previously uncharacterized domain 1B connects HEL1 domains 1A and 2A to a long linker of ZBD, which further consists of a novel RING-like module and treble-clef zinc finger, together coordinating three Zn atoms. On substrate binding, major conformational changes were evident outside the HEL1 domains, notably in domain 1B. Structural characterization, mutagenesis and biochemistry revealed that helicase activity depends on the extensive relay of interactions between the ZBD and HEL1 domains. The arterivirus helicase structurally resembles the cellular Upf1 helicase, suggesting that nidoviruses may also use their helicases for post-transcriptional quality control of their large RNA genomes.
-
-	Structural basis for the regulatory function of a complex zinc-binding domain in a replicative arterivirus helicase resembling a nonsense-mediated mRNA decay helicase.,Deng Z, Lehmann KC, Li X, Feng C, Wang G, Zhang Q, Qi X, Yu L, Zhang X, Feng W, Wu W, Gong P, Tao Y, Posthuma CC, Snijder EJ, Gorbalenya AE, Chen Z Nucleic Acids Res. 2013 Dec 24. PMID:24369429<ref>PMID:24369429</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4n0n" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:24, 28 December 2022

OCA — Wed, 28 Dec 2022 10:24:36 GMT

←Older revision		Revision as of 10:24, 28 December 2022
Line 1:		Line 1:

	==Crystal structure of Arterivirus nonstructural protein 10 (helicase)==		==Crystal structure of Arterivirus nonstructural protein 10 (helicase)==
-	<StructureSection load='4n0n' size='340' side='right' caption='[[4n0n]], [[Resolution\|resolution]] 2.00Å' scene=''>	+	<StructureSection load='4n0n' size='340' side='right'caption='[[4n0n]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4n0n]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Eav Eav~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N0N OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4N0N FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4n0n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equine_arteritis_virus_Bucyrus Equine arteritis virus Bucyrus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N0N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N0N FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <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">[[4n0o\|4n0o]]</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=4n0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n0n OCA], [https://pdbe.org/4n0n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n0n RCSB], [https://www.ebi.ac.uk/pdbsum/4n0n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n0n ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">1a-1b, nsp10, rep ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=299386 EAV])~~</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=4n0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n0n OCA], [~~http~~://pdbe.org/4n0n PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4n0n RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4n0n PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4n0n ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/RPOA_EAVBU RPOA_EAVBU]] The replicase polyprotein 1ab is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.<ref>PMID:18078692</ref> Nsp1 is essential for viral subgenomic mRNA synthesis.<ref>PMID:18078692</ref> Nsp2 cysteine proteinase which cleaves the nsp2/nsp3 site in the polyprotein. Also displays deubiquitinating and deISGylase activities. The deubiquitinating activity cleaves both ubiquitinated and ISGylated products and may therefore regulate ubiquitin and ISG15 dependent host innate immunity.<ref>PMID:18078692</ref> The 3C-like serine proteinase chain is responsible for the majority of cleavages as it cleaves the C-terminus of the polyprotein.<ref>PMID:18078692</ref> The helicase chain, which contains a zinc finger structure, displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity.<ref>PMID:18078692</ref>	+	[https://www.uniprot.org/uniprot/RPOA_EAVBU RPOA_EAVBU] The replicase polyprotein 1ab is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.<ref>PMID:18078692</ref> Nsp1 is essential for viral subgenomic mRNA synthesis.<ref>PMID:18078692</ref> Nsp2 cysteine proteinase which cleaves the nsp2/nsp3 site in the polyprotein. Also displays deubiquitinating and deISGylase activities. The deubiquitinating activity cleaves both ubiquitinated and ISGylated products and may therefore regulate ubiquitin and ISG15 dependent host innate immunity.<ref>PMID:18078692</ref> The 3C-like serine proteinase chain is responsible for the majority of cleavages as it cleaves the C-terminus of the polyprotein.<ref>PMID:18078692</ref> The helicase chain, which contains a zinc finger structure, displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity.<ref>PMID:18078692</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Eav~~]]	+	[[Category: Equine arteritis virus Bucyrus]]
-	[[Category: ~~Chen, Z~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Deng,~~ Z]]	+	[[Category: Chen Z]]
-	[[Category: ~~Arterivirus]]~~	+	[[Category: Deng Z]]
-	~~[[Category: Helicase]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Nsp10]]~~	+
-	~~[[Category: Zbd~~]]	+

OCA at 11:22, 4 August 2016

OCA — Thu, 04 Aug 2016 11:22:29 GMT

←Older revision		Revision as of 11:22, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of Arterivirus nonstructural protein 10 (helicase)==		==Crystal structure of Arterivirus nonstructural protein 10 (helicase)==
	<StructureSection load='4n0n' size='340' side='right' caption='[[4n0n]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='4n0n' size='340' side='right' caption='[[4n0n]], [[Resolution\|resolution]] 2.00Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4n0o\|4n0o]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4n0o\|4n0o]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">1a-1b, nsp10, rep ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=299386 EAV])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">1a-1b, nsp10, rep ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=299386 EAV])</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=4n0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n0n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n0n RCSB], [http://www.ebi.ac.uk/pdbsum/4n0n 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=4n0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n0n OCA], [http://pdbe.org/4n0n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n0n RCSB], [http://www.ebi.ac.uk/pdbsum/4n0n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n0n ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 4n0n" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:50, 24 December 2014

OCA — Wed, 24 Dec 2014 13:50:18 GMT

←Older revision		Revision as of 13:50, 24 December 2014
Line 8:		Line 8:
	<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=4n0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n0n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n0n RCSB], [http://www.ebi.ac.uk/pdbsum/4n0n 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=4n0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n0n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n0n RCSB], [http://www.ebi.ac.uk/pdbsum/4n0n PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/RPOA_EAVBU RPOA_EAVBU]] The replicase polyprotein 1ab is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.<ref>PMID:18078692</ref> Nsp1 is essential for viral subgenomic mRNA synthesis.<ref>PMID:18078692</ref> Nsp2 cysteine proteinase which cleaves the nsp2/nsp3 site in the polyprotein. Also displays deubiquitinating and deISGylase activities. The deubiquitinating activity cleaves both ubiquitinated and ISGylated products and may therefore regulate ubiquitin and ISG15 dependent host innate immunity.<ref>PMID:18078692</ref> The 3C-like serine proteinase chain is responsible for the majority of cleavages as it cleaves the C-terminus of the polyprotein.<ref>PMID:18078692</ref> The helicase chain, which contains a zinc finger structure, displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity.<ref>PMID:18078692</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 18:16, 21 December 2014

OCA — Sun, 21 Dec 2014 18:16:30 GMT

←Older revision		Revision as of 18:16, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4n0n\| PDB=4n0n \| SCENE= }}~~	+	==Crystal structure of Arterivirus nonstructural protein 10 (helicase)==
-	===Crystal structure of Arterivirus nonstructural protein 10 (helicase)===	+	<StructureSection load='4n0n' size='340' side='right' caption='[[4n0n]], [[Resolution\|resolution]] 2.00Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24369429}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4n0n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Eav Eav]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N0N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N0N FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <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">[[4n0o\|4n0o]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">1a-1b, nsp10, rep ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=299386 EAV])</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=4n0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n0n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n0n RCSB], [http://www.ebi.ac.uk/pdbsum/4n0n PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	All positive-stranded RNA viruses with genomes > approximately 7 kb encode helicases, which generally are poorly characterized. The core of the nidovirus superfamily 1 helicase (HEL1) is associated with a unique N-terminal zinc-binding domain (ZBD) that was previously implicated in helicase regulation, genome replication and subgenomic mRNA synthesis. The high-resolution structure of the arterivirus helicase (nsp10), alone and in complex with a polynucleotide substrate, now provides first insights into the structural basis for nidovirus helicase function. A previously uncharacterized domain 1B connects HEL1 domains 1A and 2A to a long linker of ZBD, which further consists of a novel RING-like module and treble-clef zinc finger, together coordinating three Zn atoms. On substrate binding, major conformational changes were evident outside the HEL1 domains, notably in domain 1B. Structural characterization, mutagenesis and biochemistry revealed that helicase activity depends on the extensive relay of interactions between the ZBD and HEL1 domains. The arterivirus helicase structurally resembles the cellular Upf1 helicase, suggesting that nidoviruses may also use their helicases for post-transcriptional quality control of their large RNA genomes.

-	~~==Function==~~	+	Structural basis for the regulatory function of a complex zinc-binding domain in a replicative arterivirus helicase resembling a nonsense-mediated mRNA decay helicase.,Deng Z, Lehmann KC, Li X, Feng C, Wang G, Zhang Q, Qi X, Yu L, Zhang X, Feng W, Wu W, Gong P, Tao Y, Posthuma CC, Snijder EJ, Gorbalenya AE, Chen Z Nucleic Acids Res. 2013 Dec 24. PMID:24369429<ref>PMID:24369429</ref>
-	~~[[http://www.uniprot.org/uniprot/RPOA_EAVBU RPOA_EAVBU]] The replicase polyprotein 1ab is a multifunctional protein: it contains the activities necessary~~ for the ~~transcription~~ of ~~negative stranded RNA~~, ~~leader RNA~~, ~~subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products~~.~~<ref>PMID:18078692</ref> Nsp1 is essential for viral subgenomic mRNA synthesis~~.~~<ref>~~PMID:18078692</ref> Nsp2 cysteine proteinase which cleaves the nsp2/nsp3 site in the polyprotein. Also displays deubiquitinating and deISGylase activities. The deubiquitinating activity cleaves both ubiquitinated and ISGylated products and may therefore regulate ubiquitin and ISG15 dependent host innate immunity.<ref>PMID:18078692</ref> The 3C-like serine proteinase chain is responsible for the majority of cleavages as it cleaves the C-terminus of the polyprotein.<ref>PMID:18078692</ref> The helicase chain, which contains a zinc finger structure, displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity.<ref>PMID:~~18078692~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4n0n]] is~~ a ~~1 chain structure~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4N0N OCA].~~	+	</div>
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:024369429</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
-	[[Category: Chen, Z.]]	+	</StructureSection>
-	[[Category: Deng, Z.]]	+	[[Category: Eav]]
		+	[[Category: Chen, Z]]
		+	[[Category: Deng, Z]]
	[[Category: Arterivirus]]		[[Category: Arterivirus]]
	[[Category: Helicase]]		[[Category: Helicase]]

OCA at 10:32, 8 January 2014

OCA — Wed, 08 Jan 2014 10:32:08 GMT

←Older revision		Revision as of 10:32, 8 January 2014
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4n0n\| PDB=4n0n \| SCENE= }}
		+	===Crystal structure of Arterivirus nonstructural protein 10 (helicase)===
		+	{{ABSTRACT_PUBMED_24369429}}

-	The ~~entry 4n0n~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/RPOA_EAVBU RPOA_EAVBU]] The replicase polyprotein 1ab is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products.<ref>PMID:18078692</ref> Nsp1 is essential for viral subgenomic mRNA synthesis.<ref>PMID:18078692</ref> Nsp2 cysteine proteinase which cleaves the nsp2/nsp3 site in the polyprotein. Also displays deubiquitinating and deISGylase activities. The deubiquitinating activity cleaves both ubiquitinated and ISGylated products and may therefore regulate ubiquitin and ISG15 dependent host innate immunity.<ref>PMID:18078692</ref> The 3C-like serine proteinase chain is responsible for the majority of cleavages as it cleaves the C-terminus of the polyprotein.<ref>PMID:18078692</ref> The helicase chain, which contains a zinc finger structure, displays RNA and DNA duplex-unwinding activities with 5' to 3' polarity.<ref>PMID:18078692</ref>

-	~~Authors~~: ~~Deng, Z~~.~~, Chen, Z~~.	+	==About this Structure==
		+	[[4n0n]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N0N OCA].

-	~~Description~~: ~~Crystal structure of~~ Arterivirus ~~nonstructural protein 10 (helicase)~~	+	==Reference==
		+	<ref group="xtra">PMID:024369429</ref><references group="xtra"/><references/>
		+	[[Category: Chen, Z.]]
		+	[[Category: Deng, Z.]]
		+	[[Category: Arterivirus]]
		+	[[Category: Helicase]]
		+	[[Category: Hydrolase]]
		+	[[Category: Nsp10]]
		+	[[Category: Zbd]]

OCA at 09:43, 27 November 2013

OCA — Wed, 27 Nov 2013 09:43:32 GMT

←Older revision		Revision as of 09:43, 27 November 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4n0n is ON HOLD	+	The entry 4n0n is ON HOLD until Paper Publication

	Authors: Deng, Z., Chen, Z.		Authors: Deng, Z., Chen, Z.

	Description: Crystal structure of Arterivirus nonstructural protein 10 (helicase)		Description: Crystal structure of Arterivirus nonstructural protein 10 (helicase)

OCA at 12:54, 20 November 2013

OCA — Wed, 20 Nov 2013 12:54:30 GMT

←Older revision		Revision as of 12:54, 20 November 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4n0n is ON HOLD ~~until sometime in the future~~	+	The entry 4n0n is ON HOLD

	Authors: Deng, Z., Chen, Z.		Authors: Deng, Z., Chen, Z.

	Description: Crystal structure of Arterivirus nonstructural protein 10 (helicase)		Description: Crystal structure of Arterivirus nonstructural protein 10 (helicase)

OCA at 07:38, 13 November 2013

OCA — Wed, 13 Nov 2013 07:38:33 GMT

←Older revision		Revision as of 07:38, 13 November 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4n0n is ON HOLD	+	The entry 4n0n is ON HOLD until sometime in the future

-	Authors: ~~zengqin deng~~, ~~zhongzhou chen~~	+	Authors: Deng, Z., Chen, Z.

	Description: Crystal structure of Arterivirus nonstructural protein 10 (helicase)		Description: Crystal structure of Arterivirus nonstructural protein 10 (helicase)

OCA: Protected "4n0n" [edit=sysop:move=sysop]

OCA — Thu, 10 Oct 2013 05:53:05 GMT

Protected "4n0n" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:53, 10 October 2013