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5VAP

Crystal structure of eVP30 C-terminus and eNP peptide

Summary for 5VAP
Entry DOI10.2210/pdb5vap/pdb
Related5VAO
DescriptorMinor nucleoprotein VP30, NP (3 entities in total)
Functional Keywordsfunction class, known biology activity, viral protein
Biological sourceEbola virus (ZEBOV)
More
Total number of polymer chains4
Total formula weight28340.76
Authors
XU, W.,WU, C.,Leung, D.W.,Amarasinghe, G.K. (deposition date: 2017-03-27, release date: 2017-06-21, Last modification date: 2024-03-06)
Primary citationXu, W.,Luthra, P.,Wu, C.,Batra, J.,Leung, D.W.,Basler, C.F.,Amarasinghe, G.K.
Ebola virus VP30 and nucleoprotein interactions modulate viral RNA synthesis.
Nat Commun, 8:15576-15576, 2017
Cited by
PubMed Abstract: 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.
PubMed: 28593988
DOI: 10.1038/ncomms15576
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.85 Å)
Structure validation

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数据于2025-07-16公开中

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