4r8t - Revision history

OCA at 08:59, 20 March 2024

2024-03-20T08:59:47Z

←Older revision		Revision as of 08:59, 20 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4r8t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Japanese_encephalitis_virus Japanese encephalitis virus] and [https://en.wikipedia.org/wiki/Japanese_encephalitis_virus_strain_Nakayama Japanese encephalitis virus strain Nakayama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R8T FirstGlance]. <br>		<table><tr><td colspan='2'>[[4r8t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Japanese_encephalitis_virus Japanese encephalitis virus] and [https://en.wikipedia.org/wiki/Japanese_encephalitis_virus_strain_Nakayama Japanese encephalitis virus strain Nakayama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R8T FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 2.133Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=4r8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8t OCA], [https://pdbe.org/4r8t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r8t RCSB], [https://www.ebi.ac.uk/pdbsum/4r8t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8t 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=4r8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8t OCA], [https://pdbe.org/4r8t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r8t RCSB], [https://www.ebi.ac.uk/pdbsum/4r8t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8t ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/POLG_JAEVN POLG_JAEVN] Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA (By similarity). prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated (By similarity). Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity). Non-structural protein 1 is involved in virus replication and regulation of the innate immune response. Non-structural protein 2A may be involved viral RNA replication and capsid assembly. Non-structural protein 2B is a required cofactor for the serine protease function of NS3.[PROSITE-ProRule:PRU00859] Serine protease NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity).		[https://www.uniprot.org/uniprot/POLG_JAEVN POLG_JAEVN] Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA (By similarity). prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated (By similarity). Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity). Non-structural protein 1 is involved in virus replication and regulation of the innate immune response. Non-structural protein 2A may be involved viral RNA replication and capsid assembly. Non-structural protein 2B is a required cofactor for the serine protease function of NS3.[PROSITE-ProRule:PRU00859] Serine protease NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity).
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	We describe a data collection method that uses a single crystal to solve X-ray structures by native SAD (single-wavelength anomalous diffraction). We solved the structures of 11 real-life examples, including a human membrane protein, a protein-DNA complex and a 266-kDa multiprotein-ligand complex, using this method. The data collection strategy is suitable for routine structure determination and can be implemented at most macromolecular crystallography synchrotron beamlines.
-
-	Fast native-SAD phasing for routine macromolecular structure determination.,Weinert T, Olieric V, Waltersperger S, Panepucci E, Chen L, Zhang H, Zhou D, Rose J, Ebihara A, Kuramitsu S, Li D, Howe N, Schnapp G, Pautsch A, Bargsten K, Prota AE, Surana P, Kottur J, Nair DT, Basilico F, Cecatiello V, Pasqualato S, Boland A, Weichenrieder O, Wang B, Steinmetz MO, Caffrey M, Wang M Nat Methods. 2014 Dec 15. doi: 10.1038/nmeth.3211. PMID:25506719<ref>PMID:25506719</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4r8t" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 06:45, 2 March 2023

2023-03-02T06:45:14Z

←Older revision		Revision as of 06:45, 2 March 2023
Line 3:		Line 3:
	<StructureSection load='4r8t' size='340' side='right'caption='[[4r8t]], [[Resolution\|resolution]] 2.13Å' scene=''>		<StructureSection load='4r8t' size='340' side='right'caption='[[4r8t]], [[Resolution\|resolution]] 2.13Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4r8t]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Jaevn Jaevn~~] and [~~http~~://en.wikipedia.org/wiki/~~Japanese_encephalitis~~ Japanese encephalitis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8T OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4R8T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4r8t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Japanese_encephalitis_virus Japanese encephalitis virus] and [https://en.wikipedia.org/wiki/Japanese_encephalitis_virus_strain_Nakayama Japanese encephalitis virus strain Nakayama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R8T FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NS3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11076 JAEVN]), NS3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11072 Japanese encephalitis])</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=4r8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8t OCA], [https://pdbe.org/4r8t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r8t RCSB], [https://www.ebi.ac.uk/pdbsum/4r8t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8t 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=4r8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8t OCA], [~~http~~://pdbe.org/4r8t PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4r8t RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4r8t PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8t ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/POLG_JAEVN POLG_JAEVN]] Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA (By similarity). prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated (By similarity). Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity). Non-structural protein 1 is involved in virus replication and regulation of the innate immune response. Non-structural protein 2A may be involved viral RNA replication and capsid assembly. Non-structural protein 2B is a required cofactor for the serine protease function of NS3.[PROSITE-ProRule:PRU00859] Serine protease NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity).	+	[https://www.uniprot.org/uniprot/POLG_JAEVN POLG_JAEVN] Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA (By similarity). prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated (By similarity). Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity). Non-structural protein 1 is involved in virus replication and regulation of the innate immune response. Non-structural protein 2A may be involved viral RNA replication and capsid assembly. Non-structural protein 2B is a required cofactor for the serine protease function of NS3.[PROSITE-ProRule:PRU00859] Serine protease NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Jaevn~~]]	+	[[Category: Japanese encephalitis virus]]
-	[[Category: Japanese encephalitis]]	+	[[Category: Japanese encephalitis virus strain Nakayama]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Nair~~, D T~~]]	+	[[Category: Nair DT]]
-	[[Category: Olieric, V]]	+	[[Category: Olieric V]]
-	[[Category: Wang, M]]	+	[[Category: Wang M]]
-	[[Category: Weinert, T]]	+	[[Category: Weinert T]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Ns2b]]~~	+
-	~~[[Category: Protease]]~~	+
-	~~[[Category: Serine protease~~]]	+

OCA at 09:55, 1 May 2019

2019-05-01T09:55:05Z

←Older revision		Revision as of 09:55, 1 May 2019
Line 1:		Line 1:

	==Structure of JEV protease==		==Structure of JEV protease==
-	<StructureSection load='4r8t' size='340' side='right' caption='[[4r8t]], [[Resolution\|resolution]] 2.13Å' scene=''>	+	<StructureSection load='4r8t' size='340' side='right'caption='[[4r8t]], [[Resolution\|resolution]] 2.13Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4r8t]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R8T FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4r8t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Jaevn Jaevn] and [http://en.wikipedia.org/wiki/Japanese_encephalitis Japanese encephalitis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R8T FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NS3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11076 JAEVN]), NS3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11072 Japanese encephalitis])</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=4r8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8t OCA], [http://pdbe.org/4r8t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r8t RCSB], [http://www.ebi.ac.uk/pdbsum/4r8t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8t 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=4r8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8t OCA], [http://pdbe.org/4r8t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r8t RCSB], [http://www.ebi.ac.uk/pdbsum/4r8t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8t ProSAT]</span></td></tr>
	</table>		</table>
Line 22:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Jaevn]]
		+	[[Category: Japanese encephalitis]]
		+	[[Category: Large Structures]]
	[[Category: Nair, D T]]		[[Category: Nair, D T]]
	[[Category: Olieric, V]]		[[Category: Olieric, V]]

OCA at 16:06, 17 May 2017

2017-05-17T16:06:19Z

←Older revision		Revision as of 16:06, 17 May 2017
Line 1:		Line 1:
		+
	==Structure of JEV protease==		==Structure of JEV protease==
	<StructureSection load='4r8t' size='340' side='right' caption='[[4r8t]], [[Resolution\|resolution]] 2.13Å' scene=''>		<StructureSection load='4r8t' size='340' side='right' caption='[[4r8t]], [[Resolution\|resolution]] 2.13Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[4r8t]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R8T FirstGlance]. <br>		<table><tr><td colspan='2'>[[4r8t]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R8T FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=4r8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r8t RCSB], [http://www.ebi.ac.uk/pdbsum/4r8t 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=4r8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8t OCA], [http://pdbe.org/4r8t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r8t RCSB], [http://www.ebi.ac.uk/pdbsum/4r8t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8t 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 4r8t" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:00, 14 January 2015

2015-01-14T08:00:20Z

←Older revision		Revision as of 08:00, 14 January 2015
Line 21:		Line 21:
	</StructureSection>		</StructureSection>
	[[Category: Nair, D T]]		[[Category: Nair, D T]]
-	[[Category: ~~Oligeric~~, V]]	+	[[Category: Olieric, V]]
	[[Category: Wang, M]]		[[Category: Wang, M]]
	[[Category: Weinert, T]]		[[Category: Weinert, T]]

OCA at 09:23, 31 December 2014

2014-12-31T09:23:48Z

←Older revision		Revision as of 09:23, 31 December 2014
Line 8:		Line 8:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/POLG_JAEVN POLG_JAEVN]] Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA (By similarity). prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated (By similarity). Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity). Non-structural protein 1 is involved in virus replication and regulation of the innate immune response. Non-structural protein 2A may be involved viral RNA replication and capsid assembly. Non-structural protein 2B is a required cofactor for the serine protease function of NS3.[PROSITE-ProRule:PRU00859] Serine protease NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity).		[[http://www.uniprot.org/uniprot/POLG_JAEVN POLG_JAEVN]] Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA (By similarity). prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated (By similarity). Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity). Non-structural protein 1 is involved in virus replication and regulation of the innate immune response. Non-structural protein 2A may be involved viral RNA replication and capsid assembly. Non-structural protein 2B is a required cofactor for the serine protease function of NS3.[PROSITE-ProRule:PRU00859] Serine protease NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	We describe a data collection method that uses a single crystal to solve X-ray structures by native SAD (single-wavelength anomalous diffraction). We solved the structures of 11 real-life examples, including a human membrane protein, a protein-DNA complex and a 266-kDa multiprotein-ligand complex, using this method. The data collection strategy is suitable for routine structure determination and can be implemented at most macromolecular crystallography synchrotron beamlines.
		+
		+	Fast native-SAD phasing for routine macromolecular structure determination.,Weinert T, Olieric V, Waltersperger S, Panepucci E, Chen L, Zhang H, Zhou D, Rose J, Ebihara A, Kuramitsu S, Li D, Howe N, Schnapp G, Pautsch A, Bargsten K, Prota AE, Surana P, Kottur J, Nair DT, Basilico F, Cecatiello V, Pasqualato S, Boland A, Weichenrieder O, Wang B, Steinmetz MO, Caffrey M, Wang M Nat Methods. 2014 Dec 15. doi: 10.1038/nmeth.3211. PMID:25506719<ref>PMID:25506719</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 11:09, 24 December 2014

2014-12-24T11:09:50Z

←Older revision		Revision as of 11:09, 24 December 2014
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Structure of JEV protease==
-		+	<StructureSection load='4r8t' size='340' side='right' caption='[[4r8t]], [[Resolution\|resolution]] 2.13Å' scene=''>
-	~~The entry~~ 4r8t is ~~ON HOLD~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4r8t]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R8T FirstGlance]. <br>
-	~~Authors~~: ~~Nair~~, D.T., ~~Weinert~~, T., ~~Wang~~, M., Oligeric, V.	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=4r8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r8t RCSB], [http://www.ebi.ac.uk/pdbsum/4r8t PDBsum]</span></td></tr>
-	~~Description~~: ~~Structure of JEV~~ protease	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/POLG_JAEVN POLG_JAEVN]] Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA (By similarity). prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated (By similarity). Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity). Non-structural protein 1 is involved in virus replication and regulation of the innate immune response. Non-structural protein 2A may be involved viral RNA replication and capsid assembly. Non-structural protein 2B is a required cofactor for the serine protease function of NS3.[PROSITE-ProRule:PRU00859] Serine protease NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity).
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Nair, D T]]
		+	[[Category: Oligeric, V]]
		+	[[Category: Wang, M]]
		+	[[Category: Weinert, T]]
		+	[[Category: Hydrolase]]
		+	[[Category: Ns2b]]
		+	[[Category: Protease]]
		+	[[Category: Serine protease]]

OCA at 08:25, 24 September 2014

2014-09-24T08:25:52Z

←Older revision		Revision as of 08:25, 24 September 2014
Line 3:		Line 3:
	The entry 4r8t is ON HOLD		The entry 4r8t is ON HOLD

-	Authors: Nair, D. T., Weinert, T., Wang, M., Oligeric, V.	+	Authors: Nair, D.T., Weinert, T., Wang, M., Oligeric, V.

	Description: Structure of JEV protease		Description: Structure of JEV protease

OCA: Protected "4r8t" [edit=sysop:move=sysop]

2014-09-10T08:26:40Z

Protected "4r8t" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:26, 10 September 2014

OCA: New page: '''Unreleased structure''' The entry 4r8t is ON HOLD Authors: Nair, D. T., Weinert, T., Wang, M., Oligeric, V. Description: Structure of JEV protease

2014-09-10T08:26:39Z

New page: '''Unreleased structure''' The entry 4r8t is ON HOLD Authors: Nair, D. T., Weinert, T., Wang, M., Oligeric, V. Description: Structure of JEV protease

New page

'''Unreleased structure'''

The entry 4r8t is ON HOLD

Authors: Nair, D. T., Weinert, T., Wang, M., Oligeric, V.

Description: Structure of JEV protease