6nu9

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==Crystal Structure of a Zinc-Binding Non-Structural Protein from the Hepatitis E Virus==
==Crystal Structure of a Zinc-Binding Non-Structural Protein from the Hepatitis E Virus==
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<StructureSection load='6nu9' size='340' side='right' caption='[[6nu9]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
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<StructureSection load='6nu9' size='340' side='right'caption='[[6nu9]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6nu9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NU9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NU9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6nu9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Orthohepevirus_A Orthohepevirus A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NU9 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NO2:NITRITE+ION'>NO2</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.761&#8491;</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=6nu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nu9 OCA], [http://pdbe.org/6nu9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nu9 RCSB], [http://www.ebi.ac.uk/pdbsum/6nu9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nu9 ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NO2:NITRITE+ION'>NO2</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=6nu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nu9 OCA], [https://pdbe.org/6nu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nu9 RCSB], [https://www.ebi.ac.uk/pdbsum/6nu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nu9 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/POLN_HEVPA POLN_HEVPA] Methyltransferase: Displays a capping enzyme activity. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. The enzymatic reaction involves a covalent link between 7-methyl-GMP and the methyltransferase, whereas eukaryotic capping enzymes form a covalent complex only with GMP. Methyltransferase catalyzes transfer of a methyl group from S-adenosylmethionine to GTP and GDP to yield m(7)GTP or m(7)GDP. GDP is a better substrate than GTP. This enzyme also displays guanylyltransferase activity to form a covalent complex, methyltransferase-m(7)GMP, from which 7-methyl-GMP is transferred to the mRNA to create the cap structure.[UniProtKB:Q81862] Y-domain: Indispensable for virus replication.[UniProtKB:Q81862] Putative protease: May participate in the processing of polyprotein pORF1 and capsid protein ORF2, possibly together with cellular proteases. Inhibits induction of IFN-beta by MDA5 and RIG-I pathways and down-regulates the expression of MDA5.[UniProtKB:Q81862] NTPase/helicase: Multi-functional protein that exhibits NTPase and RNA unwinding activities (By similarity). Hydrolyzes all NTPs efficiently and unwinds RNA duplexes containing 5' overhangs (By similarity). Possesses a sequence independent RNA-5'-triphosphatase (RTPase) activity suggestive of its role in forming viral cap structure. Participates also in viral genome replication, RNA translocation and genome packaging/unpackaging (By similarity).[UniProtKB:P29324][UniProtKB:Q81862] RNA-directed RNA polymerase: Plays an essential role in the virus replication (By similarity). Binds to the 3'-end of the genomic RNA to initiate viral replication (By similarity).[UniProtKB:Q81862][UniProtKB:Q9WC28]
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__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bussiere, D]]
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[[Category: Large Structures]]
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[[Category: Proudfoot, A]]
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[[Category: Orthohepevirus A]]
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[[Category: Hev]]
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[[Category: Bussiere D]]
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[[Category: Non-structural protein]]
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[[Category: Proudfoot A]]
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[[Category: Viral protein]]
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[[Category: Zinc-binding]]
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Current revision

Crystal Structure of a Zinc-Binding Non-Structural Protein from the Hepatitis E Virus

PDB ID 6nu9

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