High-resolution Crystal Structure of Dimeric VP40 From Sudan ebolavirus.
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ABSTRACT:
SUBMITTER: Clifton MC
PROVIDER: S-EPMC4564533 | biostudies-literature | 2015 Oct
REPOSITORIES: biostudies-literature
Publications
High-resolution Crystal Structure of Dimeric VP40 From Sudan ebolavirus.
Clifton Matthew C MC Bruhn Jessica F JF Atkins Kateri K Webb Terry L TL Baydo Ruth O RO Raymond Amy A Lorimer Donald D DD Edwards Thomas E TE Myler Peter J PJ Saphire Erica Ollmann EO
The Journal of infectious diseases 20150509
Ebolaviruses cause severe hemorrhagic fever. Central to the Ebola life cycle is the matrix protein VP40, which oligomerizes and drives viral budding. Here we present the crystal structure of the Sudan virus (SUDV) matrix protein. This structure is higher resolution (1.6 Å) than previously achievable. Despite differences in the protein purification, we find that it still forms a stable dimer in solution, as was noted for other Ebola VP40s. Although the N-terminal domain interface by which VP40 di ...[more]
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