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| | <StructureSection load='6eb8' size='340' side='right'caption='[[6eb8]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='6eb8' size='340' side='right'caption='[[6eb8]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6eb8]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Nipav Nipav]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EB8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EB8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6eb8]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Nipah_henipavirus Nipah henipavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EB8 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">P/V/C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=121791 NIPAV])</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]] 2.5Å</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=6eb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eb8 OCA], [http://pdbe.org/6eb8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eb8 RCSB], [http://www.ebi.ac.uk/pdbsum/6eb8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eb8 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=6eb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eb8 OCA], [https://pdbe.org/6eb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6eb8 RCSB], [https://www.ebi.ac.uk/pdbsum/6eb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6eb8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PHOSP_NIPAV PHOSP_NIPAV]] Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template (By similarity). May play a role to prevent the establishment of cellular antiviral state by binding to host STAT1 in the cytoplasm. This activity is not as strong as that of V and W. | + | [https://www.uniprot.org/uniprot/PHOSP_NIPAV PHOSP_NIPAV] Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template (By similarity). May play a role to prevent the establishment of cellular antiviral state by binding to host STAT1 in the cytoplasm. This activity is not as strong as that of V and W. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Nipav]] | + | [[Category: Nipah henipavirus]] |
| - | [[Category: Bruhn, J F]] | + | [[Category: Bruhn JF]] |
| - | [[Category: Saphire, E O]] | + | [[Category: Saphire EO]] |
| - | [[Category: Coiled coil]]
| + | |
| - | [[Category: Oligomerization]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Rna-dependent rna polymerase]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
PHOSP_NIPAV Essential component of the RNA polymerase transcription and replication complex. Binds the viral ribonucleocapsid and positions the L polymerase on the template (By similarity). May play a role to prevent the establishment of cellular antiviral state by binding to host STAT1 in the cytoplasm. This activity is not as strong as that of V and W.
Publication Abstract from PubMed
Nipah virus is a highly lethal zoonotic pathogen found in Southeast Asia that has caused human encephalitis outbreaks with 40%-70% mortality. NiV encodes its own RNA-dependent RNA polymerase within the large protein, L. Efficient polymerase activity requires the phosphoprotein, P, which tethers L to its template, the viral nucleocapsid. P is a multifunctional protein with modular domains. The central P multimerization domain is composed of a long, tetrameric coiled coil. We investigated the importance of structural features found in this domain for polymerase function using a newly constructed NiV bicistronic minigenome assay. We identified a conserved basic patch and central kink in the coiled coil that are important for polymerase function, with R555 being absolutely essential. This basic patch and central kink are conserved in the related human pathogens measles and mumps viruses, suggesting that this mechanism may be conserved.
A Conserved Basic Patch and Central Kink in the Nipah Virus Phosphoprotein Multimerization Domain Are Essential for Polymerase Function.,Bruhn JF, Hotard AL, Spiropoulou CF, Lo MK, Saphire EO Structure. 2019 Feb 13. pii: S0969-2126(19)30012-7. doi:, 10.1016/j.str.2019.01.012. PMID:30799076[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bruhn JF, Hotard AL, Spiropoulou CF, Lo MK, Saphire EO. A Conserved Basic Patch and Central Kink in the Nipah Virus Phosphoprotein Multimerization Domain Are Essential for Polymerase Function. Structure. 2019 Feb 13. pii: S0969-2126(19)30012-7. doi:, 10.1016/j.str.2019.01.012. PMID:30799076 doi:http://dx.doi.org/10.1016/j.str.2019.01.012
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