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-Structure paper
タイトル | Crystal Structure of the Herpesvirus Nuclear Egress Complex Provides Insights into Inner Nuclear Membrane Remodeling. |
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ジャーナル・号・ページ | Cell Rep, Vol. 13, Issue 12, Page 2645-2652, Year 2015 |
掲載日 | 2015年12月29日 |
著者 | Tzviya Zeev-Ben-Mordehai / Marion Weberruß / Michael Lorenz / Juliana Cheleski / Teresa Hellberg / Cathy Whittle / Kamel El Omari / Daven Vasishtan / Kyle C Dent / Karl Harlos / Kati Franzke / Christoph Hagen / Barbara G Klupp / Wolfram Antonin / Thomas C Mettenleiter / Kay Grünewald / |
PubMed 要旨 | 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 ...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. |
リンク | Cell Rep / PubMed:26711332 / PubMed Central |
手法 | X線回折 / EM (トモグラフィー) |
解像度 | 2.9 - 35 Å |
構造データ | PDB-5e8c: PDB-5fki: |
化合物 | ChemComp-ZN: ChemComp-CL: |
由来 |
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キーワード | VIRAL PROTEIN / herpesviruses / pseudorabies virus / PrV / nuclear egress / curvature / membrane remodelling / NEC / zinc finger motif / pUL31 / pUL34 / vesicle formation / trasncription / Alpha-Herpesvirinae / herpesvirus simplex / HSV-1 / Nuclear egress complex / nuclear envelope / nucleoplasmic reticulum / inner nuclear membrane / vesicle transport / nucleo-cytoplasmic transport / RYOFIB / Focused ion beam milling / FIB-SEM |