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5vap

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==Crystal structure of eVP30 C-terminus and eNP peptide==
==Crystal structure of eVP30 C-terminus and eNP peptide==
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<StructureSection load='5vap' size='340' side='right' caption='[[5vap]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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<StructureSection load='5vap' size='340' side='right'caption='[[5vap]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5vap]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VAP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VAP FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5vap]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ebola_virus Ebola virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VAP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VAP FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5vao|5vao]]</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]] 1.85&#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=5vap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vap OCA], [http://pdbe.org/5vap PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vap RCSB], [http://www.ebi.ac.uk/pdbsum/5vap PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vap ProSAT]</span></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=5vap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vap OCA], [https://pdbe.org/5vap PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vap RCSB], [https://www.ebi.ac.uk/pdbsum/5vap PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vap ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/VP30_EBOZ5 VP30_EBOZ5]] Acts as a transcription anti-termination factor immediately after transcription initiation, but does not affect transcription elongation. This function has been found to be dependent on the formation of an RNA stem-loop at the transcription start site of the first gene. Binds to RNA (By similarity).
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[https://www.uniprot.org/uniprot/VP30_EBOZ5 VP30_EBOZ5] Acts as a transcription anti-termination factor immediately after transcription initiation, but does not affect transcription elongation. This function has been found to be dependent on the formation of an RNA stem-loop at the transcription start site of the first gene. Binds to RNA (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Ebola virus (EBOV) is an enveloped negative-sense RNA virus that causes sporadic outbreaks with high case fatality rates. Ebola viral protein 30 (eVP30) plays a critical role in EBOV transcription initiation at the nucleoprotein (eNP) gene, with additional roles in the replication cycle such as viral assembly. However, the mechanistic basis for how eVP30 functions during the virus replication cycle is currently unclear. Here we define a key interaction between eVP30 and a peptide derived from eNP that is important to facilitate interactions leading to the recognition of the RNA template. We present crystal structures of the eVP30 C-terminus in complex with this eNP peptide. Functional analyses of the eVP30-eNP interface identify residues that are critical for viral RNA synthesis. Altogether, these results support a model where the eVP30-eNP interaction plays a critical role in transcription initiation and provides a novel target for the development of antiviral therapy.
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Ebola virus VP30 and nucleoprotein interactions modulate viral RNA synthesis.,Xu W, Luthra P, Wu C, Batra J, Leung DW, Basler CF, Amarasinghe GK Nat Commun. 2017 Jun 8;8:15576. doi: 10.1038/ncomms15576. PMID:28593988<ref>PMID:28593988</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5vap" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Nucleoprotein|Nucleoprotein]]
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*[[Nucleoprotein 3D structures|Nucleoprotein 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Amarasinghe, G K]]
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[[Category: Ebola virus]]
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[[Category: Leung, D W]]
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[[Category: Large Structures]]
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[[Category: WU, C]]
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[[Category: Amarasinghe GK]]
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[[Category: XU, W]]
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[[Category: Leung DW]]
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[[Category: Function class]]
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[[Category: WU C]]
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[[Category: Known biology activity]]
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[[Category: XU W]]
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[[Category: Viral protein]]
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Current revision

Crystal structure of eVP30 C-terminus and eNP peptide

PDB ID 5vap

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