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PDBsum entry 4cs8
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Viral protein
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PDB id
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4cs8
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PDB id:
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| Name: |
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Viral protein
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Title:
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Crystal structure of the asymmetric human metapneumovirus m2-1 tetramer, form 2
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Structure:
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M2-1. Chain: a, b, e. Engineered: yes. Other_details: zn ion coordinated by c7, c15, c21 and h25. M2-1. Chain: c. Engineered: yes. Other_details: zn ion coordinated by c7, c15, c21 and h25
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Source:
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Human metapneumovirus. Organism_taxid: 162145. Strain: nl1-00 (a1). Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: rosetta2.
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Resolution:
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2.10Å
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R-factor:
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0.194
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R-free:
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0.222
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Authors:
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C.Leyrat,M.Renner,K.Harlos,J.M.Grimes
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Key ref:
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C.Leyrat
et al.
(2014).
Drastic changes in conformational dynamics of the antiterminator M2-1 regulate transcription efficiency in Pneumovirinae.
Elife,
3,
e02674.
PubMed id:
DOI:
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Date:
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05-Mar-14
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Release date:
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28-May-14
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PROCHECK
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Headers
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References
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Q8QN58
(Q8QN58_9MONO) -
Protein M2-1 from Human metapneumovirus
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Seq:
Struc:
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187 a.a.
159 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Elife
3:e02674
(2014)
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PubMed id:
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Drastic changes in conformational dynamics of the antiterminator M2-1 regulate transcription efficiency in Pneumovirinae.
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C.Leyrat,
M.Renner,
K.Harlos,
J.T.Huiskonen,
J.M.Grimes.
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ABSTRACT
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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.
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Links
