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PDBsum entry 4pjs
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De novo protein, RNA binding protein
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PDB id
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4pjs
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PDB id:
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| Name: |
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De novo protein, RNA binding protein
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Title:
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Crystal structure of designed (semet)-cppr-nre protein
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Structure:
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Pentatricopeptide repeat protein. Chain: a. Engineered: yes
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Source:
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Synthetic: yes. Unidentified. Organism_taxid: 32644
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Resolution:
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2.60Å
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R-factor:
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0.188
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R-free:
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0.235
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Authors:
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S.C.Coquille,A.Filipovska,T.S.Chia,L.Rajappa,J.P.Lingford, M.F.M.Razif,S.Thore,O.Rackham
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Key ref:
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S.Coquille
et al.
(2014).
An artificial PPR scaffold for programmable RNA recognition.
Nat Commun,
5,
5729.
PubMed id:
DOI:
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Date:
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12-May-14
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Release date:
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24-Dec-14
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PROCHECK
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Headers
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References
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No UniProt id for this chain
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DOI no:
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Nat Commun
5:5729
(2014)
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PubMed id:
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An artificial PPR scaffold for programmable RNA recognition.
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S.Coquille,
A.Filipovska,
T.Chia,
L.Rajappa,
J.P.Lingford,
M.F.Razif,
S.Thore,
O.Rackham.
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ABSTRACT
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Pentatricopeptide repeat (PPR) proteins control diverse aspects of RNA
metabolism in eukaryotic cells. Although recent computational and structural
studies have provided insights into RNA recognition by PPR proteins, their
highly insoluble nature and inconsistencies between predicted and observed modes
of RNA binding have restricted our understanding of their biological functions
and their use as tools. Here we use a consensus design strategy to create
artificial PPR domains that are structurally robust and can be programmed for
sequence-specific RNA binding. The atomic structures of these artificial PPR
domains elucidate the structural basis for their stability and modelling of
RNA-protein interactions provides mechanistic insights into the importance of
RNA-binding residues and suggests modes of PPR-RNA association. The modular mode
of RNA binding by PPR proteins holds great promise for the engineering of new
tools to target RNA and to understand the mechanisms of gene regulation by
natural PPR proteins.
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Links
