PDBsum entry 5e8c

Viral protein

PDB id: 5e8c

Contents

Protein chains

238 a.a.

168 a.a.

Metals

_CL

_ZN

PDB id:

5e8c

Name:

Viral protein

Title:

Pseudorabies virus nuclear egress complex, pul31, pul34

Structure:

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

Source:

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

Resolution:

2.90Å R-factor: 0.222 R-free: 0.265

Authors:

T.Zeev-Ben-Mordehai,J.Cheleski,C.Whittle,K.El Omari,K.Harlos,C.Hagen, B.Klupp,T.C.Mettenleiter,K.Gruenewald

Key ref:

T.Zeev-Ben-Mordehai et al. (2015). Crystal Structure of the Herpesvirus Nuclear Egress Complex Provides Insights into Inner Nuclear Membrane Remodeling. Cell Rep, 13, 2645-2652. PubMed id: 26711332 DOI: 10.1016/j.celrep.2015.11.008

Date:

14-Oct-15 Release date: 23-Dec-15

Protein chain

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

Seq: 271 a.a.

Struc: 238 a.a.*

Protein chain

G3G8R3  (G3G8R3_9ALPH) -  UL34 protein from Suid herpesvirus 1

Seq: 261 a.a.

Struc: 168 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

DOI no: 10.1016/j.celrep.2015.11.008

Cell Rep 13:2645-2652 (2015)

PubMed id: 26711332

Crystal Structure of the Herpesvirus Nuclear Egress Complex Provides Insights into Inner Nuclear Membrane Remodeling.

T.Zeev-Ben-Mordehai, M.Weberruß, M.Lorenz, J.Cheleski, T.Hellberg, C.Whittle, K.El Omari, D.Vasishtan, K.C.Dent, K.Harlos, K.Franzke, C.Hagen, B.G.Klupp, W.Antonin, T.C.Mettenleiter, K.Grünewald.

ABSTRACT

Although nucleo-cytoplasmic transport is typically mediated through nuclear pore complexes, herpesvirus capsids exit the nucleus via a unique vesicular pathway. Together, the conserved herpesvirus proteins pUL31 and pUL34 form the heterodimeric nuclear egress complex (NEC), which, in turn, mediates the formation of tight-fitting membrane vesicles around capsids at the inner nuclear membrane. Here, we present the crystal structure of the pseudorabies virus NEC. The structure revealed that a zinc finger motif in pUL31 and an extensive interaction network between the two proteins stabilize the complex. Comprehensive mutational analyses, characterized both in situ and in vitro, indicated that the interaction network is not redundant but rather complementary. Fitting of the NEC crystal structure into the recently determined cryoEM-derived hexagonal lattice, formed in situ by pUL31 and pUL34, provided details on the molecular basis of NEC coat formation and inner nuclear membrane remodeling.