5TOH

Crystal Structure of the Marburg Virus VP35 Oligomerization Domain I2

5TOH の概要

• エントリーDOI: 10.2210/pdb5toh/pdb
• 関連するPDBエントリー: 5TOI
• 分子名称: Polymerase cofactor VP35 (2 entities in total)
• 機能のキーワード: polymerase cofactor, coiled coil, oligomerization, trimer, viral protein
• 由来する生物種: Lake Victoria marburgvirus (strain Musoke-80) (MARV)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 24616.79

構造登録者

Bruhn, J.F.,Kirchdoerfer, R.N.,Tickle, I.J.,Bricogne, G.,Saphire, E.O. (登録日: 2016-10-17, 公開日: 2016-11-09, 最終更新日: 2024-03-06)

主引用文献

Bruhn, J.F.,Kirchdoerfer, R.N.,Urata, S.M.,Li, S.,Tickle, I.J.,Bricogne, G.,Saphire, E.O.
Crystal Structure of the Marburg Virus VP35 Oligomerization Domain.
J. Virol., 91:-, 2017

PubMed Abstract: Marburg virus (MARV) is a highly pathogenic filovirus that is classified in a genus distinct from that of Ebola virus (EBOV) (genera Marburgvirus and Ebolavirus, respectively). Both viruses produce a multifunctional protein termed VP35, which acts as a polymerase cofactor, a viral protein chaperone, and an antagonist of the innate immune response. VP35 contains a central oligomerization domain with a predicted coiled-coil motif. This domain has been shown to be essential for RNA polymerase function. Here we present crystal structures of the MARV VP35 oligomerization domain. These structures and accompanying biophysical characterization suggest that MARV VP35 is a trimer. In contrast, EBOV VP35 is likely a tetramer in solution. Differences in the oligomeric state of this protein may explain mechanistic differences in replication and immune evasion observed for MARV and EBOV.

PubMed: 27847355
DOI: 10.1128/JVI.01085-16

実験手法

X-RAY DIFFRACTION (2.01 Å)