4CS9: Crystal Structure Of The Asymmetric Human Metapneumovirus M2-1 Tetramer Bound To Adenosine Monophosphate

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 alpha-helical tetramerization motif forming a rigid unit, followed by a flexible linker and an alpha-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.
PDB ID: 4CS9Download
MMDB ID: 120245
PDB Deposition Date: 2014/3/5
Updated in MMDB: 2014/06
Experimental Method:
x-ray diffraction
Resolution: 2.01  Å
Source Organism:
Similar Structures:
Biological Unit for 4CS9: tetrameric; determined by author and by software (PISA)
Molecular Components in 4CS9
Label Count Molecule
Proteins (4 molecules)
Molecule annotation
Molecule annotation
Chemicals (8 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB