5E8C
pseudorabies virus nuclear egress complex, pUL31, pUL34
5E8C の概要
エントリーDOI | 10.2210/pdb5e8c/pdb |
分子名称 | UL31, UL34 protein, ZINC ION, ... (4 entities in total) |
機能のキーワード | herpesviruses, pseudorabies virus, prv, nuclear egress, curvature, membrane remodelling, nec, zinc finger motif, pul31, pul34, vesicle formation, trasncription, viral protein |
由来する生物種 | Suid herpesvirus 1 (Pseudorabies virus) 詳細 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 47147.84 |
構造登録者 | Zeev-Ben-Mordehai, T.,Cheleski, J.,Whittle, C.,El Omari, K.,Harlos, K.,Hagen, C.,Klupp, B.,Mettenleiter, T.C.,Gruenewald, K. (登録日: 2015-10-14, 公開日: 2015-12-23, 最終更新日: 2024-10-16) |
主引用文献 | Zeev-Ben-Mordehai, T.,Weberru, M.,Lorenz, M.,Cheleski, J.,Hellberg, T.,Whittle, C.,El Omari, K.,Vasishtan, D.,Dent, K.C.,Harlos, K.,Franzke, K.,Hagen, C.,Klupp, B.G.,Antonin, W.,Mettenleiter, T.C.,Grunewald, K. Crystal Structure of the Herpesvirus Nuclear Egress Complex Provides Insights into Inner Nuclear Membrane Remodeling. Cell Rep, 13:2645-2652, 2015 Cited by 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: 26711332DOI: 10.1016/j.celrep.2015.11.008 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.9 Å) |
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