4ZXS

HSV-1 nuclear egress complex

Summary for 4ZXS

• Entry DOI: 10.2210/pdb4zxs/pdb
• Descriptor: Virion egress protein UL34, Virion egress protein UL31, NICKEL (II) ION, ... (7 entities in total)
• Functional Keywords: hsv-1, nuclear egress, ul31, ul34, membrane deformation, viral protein
• Biological source: Human herpesvirus 1 (HHV-1); More
• Total number of polymer chains: 4
• Total formula weight: 97938.55

Authors

Bigalke, J.M.,Heldwein, E.E. (deposition date: 2015-05-20, release date: 2015-11-11, Last modification date: 2024-10-16)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.772 Å)