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Structure of the Reston ebolavirus VP30 C‐terminal domain
Author(s) -
Clifton Matthew C.,
Kirchdoerfer Robert N.,
Atkins Kateri,
Abendroth Jan,
Raymond Amy,
Grice Rena,
Barnes Steve,
Moen Spencer,
Lorimer Don,
Edwards Thomas E.,
Myler Peter J.,
Saphire Erica Ollmann
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14003811
Subject(s) - ebolavirus , chemistry , ebola virus , terminal (telecommunication) , virology , biology , computer science , virus , telecommunications
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.