6GBR
Crystal Structure of the oligomerization domain of VP35 from Reston virus, mercury derivative
Summary for 6GBR
| Entry DOI | 10.2210/pdb6gbr/pdb |
| Descriptor | Polymerase cofactor VP35, MERCURIBENZOIC ACID (2 entities in total) |
| Functional Keywords | coiled-coil, viral protein |
| Biological source | Reston ebolavirus |
| Total number of polymer chains | 4 |
| Total formula weight | 32844.43 |
| 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: 2024-05-08) |
| 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 Cited by 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: 30482729DOI: 10.1016/j.str.2018.09.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.15 Å) |
Structure validation
Download full validation report
