4Z3U

PRV nuclear egress complex

4Z3U の概要

• エントリーDOI: 10.2210/pdb4z3u/pdb
• 分子名称: UL34 protein, UL31, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: complex, membrane binding, viral protein
• 由来する生物種: Suid herpesvirus 1 (Pseudorabies virus); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 98340.17

構造登録者

Bigalke, J.M.,Heldwein, E.E. (登録日: 2015-03-31, 公開日: 2015-11-11, 最終更新日: 2024-10-16)

主引用文献

Bigalke, J.M.,Heldwein, E.E.
Structural basis of membrane budding by the nuclear egress complex of herpesviruses.
Embo J., 34:2921-2936, 2015

PubMed Abstract: During nuclear egress, herpesvirus capsids bud at the inner nuclear membrane forming perinuclear viral particles that subsequently fuse with the outer nuclear membrane, releasing capsids into the cytoplasm. This unusual budding process is mediated by the nuclear egress complex (NEC) composed of two conserved viral proteins, UL31 and UL34. Earlier, we discovered that the herpesvirus nuclear egress complex (NEC) could bud synthetic membranes in vitro without the help of other proteins by forming a coat-like hexagonal scaffold inside the budding membrane. To understand the structural basis of NEC-mediated membrane budding, we determined the crystal structures of the NEC from two herpesviruses. The hexagonal lattice observed in the NEC crystals recapitulates the honeycomb coats within the budded vesicles. Perturbation of the oligomeric interfaces through mutagenesis blocks budding in vitro confirming that NEC oligomerization into a honeycomb lattice drives budding. The structure represents the first atomic-level view of an oligomeric array formed by a membrane-deforming protein, making possible the dissection of its unique budding mechanism and the design of inhibitors to block it.

PubMed: 26511020
DOI: 10.15252/embj.201592359

実験手法

X-RAY DIFFRACTION (2.706 Å)