4r8t

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<StructureSection load='4r8t' size='340' side='right'caption='[[4r8t]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
<StructureSection load='4r8t' size='340' side='right'caption='[[4r8t]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<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>
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</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>
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</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>
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<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>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=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>
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</table>
</table>
== Function ==
== Function ==
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[[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).
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[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 ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Jaevn]]
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[[Category: Japanese encephalitis virus]]
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[[Category: Japanese encephalitis]]
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[[Category: Japanese encephalitis virus strain Nakayama]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Nair, D T]]
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[[Category: Nair DT]]
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[[Category: Olieric, V]]
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[[Category: Olieric V]]
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[[Category: Wang, M]]
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[[Category: Wang M]]
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[[Category: Weinert, T]]
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[[Category: Weinert T]]
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[[Category: Hydrolase]]
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[[Category: Ns2b]]
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[[Category: Protease]]
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[[Category: Serine protease]]
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Revision as of 06:45, 2 March 2023

Structure of JEV protease

PDB ID 4r8t

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