PDBsum entry 4z3u

Viral protein

PDB id: 4z3u

Contents

Protein chains

168 a.a.

252 a.a.

Metals

_CL ×5

_ZN ×2

_NA

Waters ×38

PDB id:

4z3u

Name:

Viral protein

Title:

Prv nuclear egress complex

Structure:

Ul34 protein. Chain: a, c. Engineered: yes. Ul31. Chain: b, d. Synonym: ul31 protein. Engineered: yes

Source:

Suid herpesvirus 1. Pseudorabies virus. Organism_taxid: 10345. Gene: ul34. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: ul31. Expression_system_taxid: 562

Resolution:

2.71Å R-factor: 0.217 R-free: 0.273

Authors:

J.M.Bigalke,E.E.Heldwein

Key ref:

J.M.Bigalke and E.E.Heldwein (2015). Structural basis of membrane budding by the nuclear egress complex of herpesviruses. Embo J, 34, 2921-2936. PubMed id: 26511020 DOI: 10.15252/embj.201592359

Date:

31-Mar-15 Release date: 11-Nov-15

Protein chains

G3G8X8  (G3G8X8_9ALPH) -  UL34 from Suid herpesvirus 1

Seq: 262 a.a.

Struc: 168 a.a.*

Protein chains

G3G955  (G3G955_9ALPH) -  Nuclear egress lamina protein from Suid herpesvirus 1

Seq: 271 a.a.

Struc: 252 a.a.

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.15252/embj.201592359

Embo J 34:2921-2936 (2015)

PubMed id: 26511020

Structural basis of membrane budding by the nuclear egress complex of herpesviruses.

J.M.Bigalke, E.E.Heldwein.

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.