2MJZ

Capsid model of M13 bacteriophage virus from Magic-angle spinning NMR and Rosetta modeling

2MJZ の概要

• エントリーDOI: 10.2210/pdb2mjz/pdb
• NMR情報: BMRB: 19747
• 分子名称: Capsid protein G8P (1 entity in total)
• 機能のキーワード: molecular assembly, viral protein
• 由来する生物種: Enterobacteria phage M13
• 細胞内の位置: Virion: P69541
• タンパク質・核酸の鎖数: 35
• 化学式量合計: 183505.49

構造登録者

Morag, O.,Sgourakis, N.G.,Baker, D.,Goldbourt, A. (登録日: 2014-01-22, 公開日: 2015-01-07, 最終更新日: 2024-05-01)

主引用文献

Morag, O.,Sgourakis, N.G.,Baker, D.,Goldbourt, A.
The NMR-Rosetta capsid model of M13 bacteriophage reveals a quadrupled hydrophobic packing epitope.
Proc.Natl.Acad.Sci.USA, 112:971-976, 2015

PubMed Abstract: Filamentous phage are elongated semiflexible ssDNA viruses that infect bacteria. The M13 phage, belonging to the family inoviridae, has a length of ∼1 μm and a diameter of ∼7 nm. Here we present a structural model for the capsid of intact M13 bacteriophage using Rosetta model building guided by structure restraints obtained from magic-angle spinning solid-state NMR experimental data. The C5 subunit symmetry observed in fiber diffraction studies was enforced during model building. The structure consists of stacked pentamers with largely alpha helical subunits containing an N-terminal type II β-turn; there is a rise of 16.6-16.7 Å and a tilt of 36.1-36.6° between consecutive pentamers. The packing of the subunits is stabilized by a repeating hydrophobic stacking pocket; each subunit participates in four pockets by contributing different hydrophobic residues, which are spread along the subunit sequence. Our study provides, to our knowledge, the first magic-angle spinning NMR structure of an intact filamentous virus capsid and further demonstrates the strength of this technique as a method of choice to study noncrystalline, high-molecular-weight molecular assemblies.

PubMed: 25587134
DOI: 10.1073/pnas.1415393112

実験手法

SOLID-STATE NMR