4PJS

Crystal structure of designed (SeMet)-cPPR-NRE protein

Summary for 4PJS

• Entry DOI: 10.2210/pdb4pjs/pdb
• Related: 4PJQ 4PJR
• Descriptor: Pentatricopeptide repeat protein, CALCIUM ION (3 entities in total)
• Functional Keywords: designer rna-binding proteins; pentatricopeptide repeat; synthetic biology; rna-protein interactions, rna binding protein, de novo protein
• Biological source: unidentified
• Total number of polymer chains: 1
• Total formula weight: 33335.14

Authors

Coquille, S.C.,Filipovska, A.,Chia, T.S.,Rajappa, L.,Lingford, J.P.,Razif, M.F.M.,Thore, S.,Rackham, O. (deposition date: 2014-05-12, release date: 2014-12-24, Last modification date: 2024-10-16)

Primary citation

Coquille, S.,Filipovska, A.,Chia, T.,Rajappa, L.,Lingford, J.P.,Razif, M.F.,Thore, S.,Rackham, O.
An artificial PPR scaffold for programmable RNA recognition.
Nat Commun, 5:5729-5729, 2014

PubMed Abstract: 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.

PubMed: 25517350
DOI: 10.1038/ncomms6729

Experimental method

X-RAY DIFFRACTION (2.6 Å)