More than Meets the Eye: Hidden Structures in the Proteome: Video 2

A video from the 2016 review by Hal Wasserman and Erica Ollmann Saphire, "More than Meets the Eye: Hidden Structures in the Proteome," from the Annual Review of Virology.

Shown: Morphs modeling how the VP40 dimer might transition to the matrix-assembling linear hexamer (Video 1) and the RNA-binding octameric ring (this video). In each of these videos, N-terminal domains are blue and C-terminal domains are orange. In Video 1, construction of the hexamer form the dimer, it is modeled that three VP40 dimers gather at the membrane surface. It is hypothesized that an electrostatic interaction with lipid head groups triggers conformational rearrangement and assembly of the hexamer. Note that in the crystal structure of this hexamer (PDB: 4LDD), the central VP40 is upside down. In this video, the crystal structure of the octameric ring (PDB: 1H2D; Gomis-Ruth et al. 2003, Structure 11:423–33) reveals a 3-nt RNA bound to each N-terminal domain. RNA is illustrated here as the trigger that begins the conformational rearrangement. However, it is not yet known what the trigger of this rearrangement is. We thank Dr. Zachary Bornholdt for the use of these models and videos, originally published as supplemental figures in Bornholdt et al. 2013, Cell 154:763–74.