3V7O

Crystal structure of the C-terminal domain of Ebola virus VP30 (strain Reston-89)

Summary for 3V7O

• Entry DOI: 10.2210/pdb3v7o/pdb
• Descriptor: Minor nucleoprotein VP30, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: ebola, vp30, ssgcid, seattle structural genomics center for infectious disease, smt, nucleoprotein, transcription
• Biological source: Reston ebolavirus (REBOV)
• Cellular location: Virion: Q8JPX6
• Total number of polymer chains: 2
• Total formula weight: 51694.73

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2011-12-21, release date: 2012-02-08, Last modification date: 2025-10-22)

Primary citation

Clifton, M.C.,Kirchdoerfer, R.N.,Atkins, K.,Abendroth, J.,Raymond, A.,Grice, R.,Barnes, S.,Moen, S.,Lorimer, D.,Edwards, T.E.,Myler, P.J.,Saphire, E.O.
Structure of the Reston ebolavirus VP30 C-terminal domain.
Acta Crystallogr F Struct Biol Commun, 70:457-460, 2014

PubMed Abstract: 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.

PubMed: 24699737
DOI: 10.1107/S2053230X14003811

Experimental method

X-RAY DIFFRACTION (2.25 Å)