Structural highlights
Function
[VP30_EBORR] 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).
Publication Abstract from PubMed
The ebolaviruses can cause severe hemorrhagic fever. Essential to the ebolavirus life cycle is the protein VP30, which serves as a transcriptional cofactor. Here, the crystal structure of the C-terminal, NP-binding domain of VP30 from Reston ebolavirus is presented. Reston VP30 and Ebola VP30 both form homodimers, but the dimeric interfaces are rotated relative to each other, suggesting subtle inherent differences or flexibility in the dimeric interface.
Structure of the Reston ebolavirus VP30 C-terminal domain.,Clifton MC, Kirchdoerfer RN, Atkins K, Abendroth J, Raymond A, Grice R, Barnes S, Moen S, Lorimer D, Edwards TE, Myler PJ, Saphire EO Acta Crystallogr F Struct Biol Commun. 2014 Apr;70(Pt 4):457-60. doi:, 10.1107/S2053230X14003811. Epub 2014 Mar 25. PMID:24699737[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Clifton MC, Kirchdoerfer RN, Atkins K, Abendroth J, Raymond A, Grice R, Barnes S, Moen S, Lorimer D, Edwards TE, Myler PJ, Saphire EO. Structure of the Reston ebolavirus VP30 C-terminal domain. Acta Crystallogr F Struct Biol Commun. 2014 Apr;70(Pt 4):457-60. doi:, 10.1107/S2053230X14003811. Epub 2014 Mar 25. PMID:24699737 doi:http://dx.doi.org/10.1107/S2053230X14003811
