4JNH

A unique spumavirus gag N-terminal domain with functional properties of orthoretroviral Matrix and Capsid

4JNH の概要

• エントリーDOI: 10.2210/pdb4jnh/pdb
• 関連するPDBエントリー: 4JMR
• 分子名称: Gag polyprotein (2 entities in total)
• 機能のキーワード: gag, coiled-coil, viral protein, env
• 由来する生物種: Human spumaretrovirus (SFVcpz(hu))
• 細胞内の位置: Gag protein: Virion. p3: Virion: P14349
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46485.91

構造登録者

Taylor, I.A.,Goldstone, D.C.,Flower, T.G.,Ball, N.J. (登録日: 2013-03-15, 公開日: 2013-05-29, 最終更新日: 2024-10-30)

主引用文献

Goldstone, D.C.,Flower, T.G.,Ball, N.J.,Sanz-Ramos, M.,Yap, M.W.,Ogrodowicz, R.W.,Stanke, N.,Reh, J.,Lindemann, D.,Stoye, J.P.,Taylor, I.A.
A Unique Spumavirus Gag N-terminal Domain with Functional Properties of Orthoretroviral Matrix and Capsid.
Plos Pathog., 9:e1003376-e1003376, 2013

PubMed Abstract: The Spumaretrovirinae, or foamyviruses (FVs) are complex retroviruses that infect many species of monkey and ape. Although FV infection is apparently benign, trans-species zoonosis is commonplace and has resulted in the isolation of the Prototypic Foamy Virus (PFV) from human sources and the potential for germ-line transmission. Despite little sequence homology, FV and orthoretroviral Gag proteins perform equivalent functions, including genome packaging, virion assembly, trafficking and membrane targeting. In addition, PFV Gag interacts with the FV Envelope (Env) protein to facilitate budding of infectious particles. Presently, there is a paucity of structural information with regards FVs and it is unclear how disparate FV and orthoretroviral Gag molecules share the same function. Therefore, in order to probe the functional overlap of FV and orthoretroviral Gag and learn more about FV egress and replication we have undertaken a structural, biophysical and virological study of PFV-Gag. We present the crystal structure of a dimeric amino terminal domain from PFV, Gag-NtD, both free and in complex with the leader peptide of PFV Env. The structure comprises a head domain together with a coiled coil that forms the dimer interface and despite the shared function it is entirely unrelated to either the capsid or matrix of Gag from other retroviruses. Furthermore, we present structural, biochemical and virological data that reveal the molecular details of the essential Gag-Env interaction and in addition we also examine the specificity of Trim5α restriction of PFV. These data provide the first information with regards to FV structural proteins and suggest a model for convergent evolution of gag genes where structurally unrelated molecules have become functionally equivalent.

PubMed: 23675305
DOI: 10.1371/journal.ppat.1003376

実験手法

X-RAY DIFFRACTION (2.402 Å)