5FKI

Pseudorabies virus (PrV) nuclear egress complex proteins fitted as a hexameric lattice into a sub-tomogram average derived from focused- ion beam milled lamellae electron cryo-microscopic data

This is a non-PDB format compatible entry.

Summary for 5FKI

• Entry DOI: 10.2210/pdb5fki/pdb
• EMDB information: 3197
• Descriptor: UL31, UL34 protein, ZINC ION, ... (4 entities in total)
• Functional Keywords: alpha-herpesvirinae, herpesvirus simplex, hsv-1, pseudorabies virus, prv, nuclear egress complex, nuclear envelope, nucleoplasmic reticulum, inner nuclear membrane, vesicle transport, nucleo-cytoplasmic transport, ryofib, focused ion beam milling, fib-sem, viral protein
• Biological source: Suid herpesvirus 1 (Pseudorabies virus); More
• Total number of polymer chains: 84
• Total formula weight: 2042224.21

Authors

Hagen, C.,Dent, K.C.,Zeev Ben Mordehai, T.,Vasishtan, D.,Antonin, W.,Mettenleiter, T.C.,Gruenewald, K. (deposition date: 2015-10-16, release date: 2016-03-16, Last modification date: 2024-10-23)

Primary citation

Zeev Ben Mordehai, T.,Weberruss, M.,Lorenz, M.,Cheleski, J.,Hellberg, T.,Whittle, C.,El Omari, K.,Vasishtan, D.,Dent, K.C.,Harlos, K.,Hagen, C.,Klupp, B.G.,Antonin, W.,Mettenleiter, T.C.,Gruenewald, K.
Crystal Structure of the Herpesvirus Nuclear Egress Complex Provides Insights Into Inner Nuclear Membrane Remodelling
Cell Rep., 13:2645-2652, 2015

PubMed 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.

PubMed: 26711332
DOI: 10.1016/j.celrep.2015.11.008

Experimental method

ELECTRON MICROSCOPY (35 Å)