4PJS: Crystal structure of designed (SeMet)-cPPR-NRE protein

Citation:
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.
PDB ID: 4PJSDownload
MMDB ID: 125874
PDB Deposition Date: 2014/5/12
Updated in MMDB: 2017/12
Experimental Method:
x-ray diffraction
Resolution: 2.6  Å
Similar Structures:
Biological Unit for 4PJS: monomeric; determined by author and by software (PISA)
Molecular Components in 4PJS
Label Count Molecule
Protein (1 molecule)
1
Pentatricopeptide Repeat Protein
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

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