Poster Presentation The 48th Lorne Conference on Protein Structure and Function 2023

Refinement of AlphaFold models of RNA editing factors using Small Angle X-ray Scattering (#418)

Santana Royan 1 , Charlie Bond 2 , Ian Small 2 3
  1. CSIRO Advanced Engineering Biology Future Science Platform, Canberra, ACT, Australia
  2. School of Chemistry and Biochemistry, The University of Western Australia, Crawley, WA, Australia
  3. ARC Centre of Excellence for Innovations in Synthetic Biology, Research School of Chemistry, Australian National University, Canberra, ACT, Australia

Members of the pentatricopeptide repeat (PPR) protein family catalyse targeted cytidine to uridine RNA editing in land plants. These proteins contain of a scaffold of helix-turn-helix PPR domains, which recognise RNA in a single domain to single base manner following a well-elucidated code. A cytidine deaminase-like domain at the C-terminus of some PPR editing factors is the catalytic domain in the process. AlphaFold 2 has provided the first structural model of a full-length PPR RNA editing enzyme designed in silico. Here, we describe the refinement and evaluation of this model against Small Angle X-ray Scattering data, as well as that of models with a plant supplementary factor and its target RNA.