4CS7

Crystal structure of the asymmetric human metapneumovirus M2-1 tetramer, form 1

Summary for 4CS7

• Entry DOI: 10.2210/pdb4cs7/pdb
• Related: 4CS8 4CS9 4CSA
• Descriptor: M2-1, ZINC ION (3 entities in total)
• Functional Keywords: viral protein, antiterminator, transcription elongation, rna-binding, modular protein, asymmetric tetramer
• Biological source: HUMAN METAPNEUMOVIRUS
• Total number of polymer chains: 4
• Total formula weight: 85998.70

Authors

Leyrat, C.,Renner, M.,Harlos, K.,Grimes, J.M. (deposition date: 2014-03-05, release date: 2014-05-28, Last modification date: 2024-05-08)

Primary citation

Leyrat, C.,Renner, M.,Harlos, K.,Huiskonen, J.T.,Grimes, J.M.
Drastic Changes in Conformational Dynamics of the Antiterminator M2-1 Regulate Transcription Efficiency in Pneumovirinae.
Elife, 3:02674-, 2014

PubMed 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.

PubMed: 24842877
DOI: 10.7554/ELIFE.02674

Experimental method

X-RAY DIFFRACTION (2.47 Å)