 |
PDBsum entry 4cs8
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Viral protein
|
PDB id
|
|
|
|
4cs8
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Drastic changes in conformational dynamics of the antiterminator m2-1 regulate transcription efficiency in pneumovirinae.
|
|
|
Authors
|
|
C.Leyrat,
M.Renner,
K.Harlos,
J.T.Huiskonen,
J.M.Grimes.
|
|
|
Ref.
|
|
Elife, 2014,
3,
e02674.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The M2-1 protein of human metapneumovirus (HMPV) is a zinc-binding transcription
antiterminator which is highly conserved among pneumoviruses. We report the
structure of tetrameric HMPV M2-1. Each protomer features a N-terminal zinc
finger domain and an α-helical tetramerization motif forming a rigid unit,
followed by a flexible linker and an α-helical core domain. The tetramer is
asymmetric, three of the protomers exhibiting a closed conformation, and one an
open conformation. Molecular dynamics simulations and SAXS demonstrate a dynamic
equilibrium between open and closed conformations in solution. Structures of
adenosine monophosphate- and DNA- bound M2-1 establish the role of the zinc
finger domain in base-specific recognition of RNA. Binding to 'gene end' RNA
sequences stabilized the closed conformation of M2-1 leading to a drastic shift
in the conformational landscape of M2-1. We propose a model for recognition of
gene end signals and discuss the implications of these findings for
transcriptional regulation in pneumoviruses.DOI:
http://dx.doi.org/10.7554/eLife.02674.001.
|
|
|
|
|
|
|
