3TCQ

Crystal Structure of matrix protein VP40 from Ebola virus Sudan

Summary for 3TCQ

• Entry DOI: 10.2210/pdb3tcq/pdb
• Descriptor: Matrix protein VP40 (2 entities in total)
• Functional Keywords: seattle structural genomics centers for infectious disease, ssgcid, ebola, sebov, seattle structural genomics center for infectious disease, matrix protein, viral protein
• Biological source: Sudan ebolavirus
• Total number of polymer chains: 1
• Total formula weight: 35513.23

Authors

Clifton, M.C.,Edwards, T.E.,Anderson, V.,Atkins, K.,Raymond, A.,Saphire, E.O.,Seattle Structural Genomics Center for Infectious Disease,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2011-08-09, release date: 2012-10-03, Last modification date: 2023-09-13)

Primary citation

Clifton, M.C.,Bruhn, J.F.,Atkins, K.,Webb, T.L.,Baydo, R.O.,Raymond, A.,Lorimer, D.D.,Edwards, T.E.,Myler, P.J.,Saphire, E.O.
High-resolution Crystal Structure of Dimeric VP40 From Sudan ebolavirus.
J Infect Dis, 212 Suppl 2:S167-S171, 2015

PubMed Abstract: 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 dimerizes is conserved between Ebola virus and SUDV, the C-terminal domain interface by which VP40 dimers may further assemble is significantly smaller in this SUDV assembly.

PubMed: 25957961
DOI: 10.1093/infdis/jiv090

Experimental method

X-RAY DIFFRACTION (1.6 Å)