4Z9P

Crystal structure of Ebola virus nucleoprotein core domain at 1.8A resolution

4Z9P の概要

• エントリーDOI: 10.2210/pdb4z9p/pdb
• 分子名称: Nucleoprotein (2 entities in total)
• 機能のキーワード: ebola, filoviridae, nucleoprotein, rna binding protein, viral protein
• 由来する生物種: Zaire ebolavirus (strain Mayinga-76) (ZEBOV)
• 細胞内の位置: Virion: P18272
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35128.46

構造登録者

Guo, Y.,Dong, S.S.,Yang, P.,Li, G.B.,Liu, B.C.,Yang, C.,Rao, Z.H. (登録日: 2015-04-11, 公開日: 2015-05-20, 最終更新日: 2024-03-20)

主引用文献

Dong, S.,Yang, P.,Li, G.,Liu, B.,Wang, W.,Liu, X.,Xia, B.,Yang, C.,Lou, Z.,Guo, Y.,Rao, Z.
Insight into the Ebola virus nucleocapsid assembly mechanism: crystal structure of Ebola virus nucleoprotein core domain at 1.8 A resolution.
Protein Cell, 6:351-362, 2015

PubMed Abstract: Ebola virus (EBOV) is a key member of Filoviridae family and causes severe human infectious diseases with high morbidity and mortality. As a typical negative-sense single-stranded RNA (-ssRNA) viruses, EBOV possess a nucleocapsid protein (NP) to facilitate genomic RNA encapsidation to form viral ribonucleoprotein complex (RNP) together with genome RNA and polymerase, which plays the most essential role in virus proliferation cycle. However, the mechanism of EBOV RNP formation remains unclear. In this work, we solved the high resolution structure of core domain of EBOV NP. The polypeptide of EBOV NP core domain (NP(core)) possesses an N-lobe and C-lobe to clamp a RNA binding groove, presenting similarities with the structures of the other reported viral NPs encoded by the members from Mononegavirales order. Most strikingly, a hydrophobic pocket at the surface of the C-lobe is occupied by an α-helix of EBOV NP(core) itself, which is highly conserved among filoviridae family. Combined with other biochemical and biophysical evidences, our results provides great potential for understanding the mechanism underlying EBOV RNP formation via the mobility of EBOV NP element and enables the development of antiviral therapies targeting EBOV RNP formation.

PubMed: 25910597
DOI: 10.1007/s13238-015-0163-3

実験手法

X-RAY DIFFRACTION (1.792 Å)