6GBO

Crystal Structure of the oligomerization domain of Vp35 from Ebola virus

6GBO の概要

• エントリーDOI: 10.2210/pdb6gbo/pdb
• 分子名称: Polymerase cofactor VP35 (2 entities in total)
• 機能のキーワード: coiled-coil, viral protein
• 由来する生物種: Ebola virus (ZEBOV)
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 99232.80

構造登録者

Zinzula, L.,Nagy, I.,Orsini, M.,Weyher-Stingl, E.,Baumeister, W.,Bracher, A. (登録日: 2018-04-16, 公開日: 2018-10-10, 最終更新日: 2024-01-17)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.1 Å)