6GBQ

Crystal Structure of the oligomerization domain of Vp35 from Reston virus

Summary for 6GBQ

• Entry DOI: 10.2210/pdb6gbq/pdb
• Descriptor: Polymerase cofactor VP35 (2 entities in total)
• Functional Keywords: coiled-coil, viral protein
• Biological source: Reston ebolavirus
• Total number of polymer chains: 8
• Total formula weight: 64402.05

Authors

Zinzula, L.,Nagy, I.,Orsini, M.,Weyher-Stingl, E.,Baumeister, W.,Bracher, A. (deposition date: 2018-04-16, release date: 2018-10-10, Last modification date: 2024-01-17)

Primary citation

Zinzula, L.,Nagy, I.,Orsini, M.,Weyher-Stingl, E.,Bracher, A.,Baumeister, W.
Structures of Ebola and Reston Virus VP35 Oligomerization Domains and Comparative Biophysical Characterization in All Ebolavirus Species.
Structure, 27:39-54.e6, 2019

PubMed Abstract: The multifunctional virion protein 35 (VP35) of ebolaviruses is a critical determinant of virulence and pathogenesis indispensable for viral replication and host innate immune evasion. Essential for VP35 function is homo-oligomerization via a coiled-coil motif. Here we report crystal structures of VP35 oligomerization domains from the prototypic Ebola virus (EBOV) and the non-pathogenic Reston virus (RESTV), together with a comparative biophysical characterization of the domains from all known species of the Ebolavirus genus. EBOV and RESTV VP35 oligomerization domains form bipartite parallel helix bundles with a canonical coiled coil in the N-terminal half and increased plasticity in the highly conserved C-terminal half. The domain assembles into trimers and tetramers in EBOV, whereas it exclusively forms tetramers in all other ebolavirus species. Substitution of coiled-coil leucine residues critical for immune antagonism leads to aberrant oligomerization. A conserved arginine involved in inter-chain salt bridges stabilizes the VP35 oligomerization domain and modulates between coiled-coil oligomeric states.

PubMed: 30482729
DOI: 10.1016/j.str.2018.09.009

Experimental method

X-RAY DIFFRACTION (2.43 Å)