2i8b | pdb_00002i8b

Crystal structure of the C-terminal domain of Ebola virus VP30

spinqualitylabelsall models 2i8b, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2i8b is a 2 chain structure with sequence from Zebov. The October 2014 RCSB PDB Molecule of the Month feature on Ebola Virus Proteins by David Goodsell is 10.2210/rcsb_pdb/mom_2014_10. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: MSE Gene: VP30 (ZEBOV) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [VP30_EBOZM] 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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Transcription of the highly pathogenic Ebola virus depends on VP30, a nucleocapsid-associated Ebola virus-specific transcription factor. The transcription activator VP30 was shown to play an essential role in Ebola virus replication, most likely by stabilizing nascent mRNA. Here we present the crystal structure of the C-terminal domain (CTD) of VP30 (VP30(CTD)) at 2.0-A resolution. VP30(CTD) folds independently into a dimeric helical assembly. The VP30(CTD) dimers assemble into hexamers that are present in virions, by an oligomerization domain located in the N terminus of VP30. Mutagenesis of conserved charged amino acids on VP30(CTD) revealed that two regions, namely a basic cluster around Lys-180 and Glu-197, are required for nucleocapsid interaction. However, only mutagenesis of the basic cluster was shown to impair transcription activation, suggesting that both processes are regulated independently. The structure and the mutagenesis results reveal a potential pocket for small-molecule inhibitors that might prevent VP30 activity and thus virus propagation as it has been shown previously by peptides, which interfere with VP30 homooligomerization. Crystal structure of the C-terminal domain of Ebola virus VP30 reveals a role in transcription and nucleocapsid association.,Hartlieb B, Muziol T, Weissenhorn W, Becker S Proc Natl Acad Sci U S A. 2007 Jan 9;104(2):624-9. Epub 2007 Jan 3. PMID:17202263 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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