Crystal structures of a series of RNA aptamers complexed to the same protein target

Nat Struct Biol. 1998 Nov;5(11):970-5. doi: 10.1038/2946.

Abstract

We have determined the crystal structures, at 2.8 A resolution, of two different RNA aptamers, each bound to MS2 coat protein. One of the aptamers contains a non-Watson-Crick base pair, while the other is missing one of the unpaired adenines that make sequence-specific contacts in the wild-type complex. Despite these differences, the RNA aptamers bind in the same location on the protein as the wild-type translational operator. Comparison of these new structures with other MS2-RNA complexes allows us to refine further the definition of the minimal recognition elements and suggests a possible application of the MS2 system for routine structure determination of small nucleic acid motifs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Pairing
  • Capsid / chemistry*
  • Capsid Proteins*
  • Crystallography, X-Ray
  • Hydrogen Bonding
  • Models, Molecular
  • Nucleic Acid Conformation*
  • RNA / chemistry*
  • RNA-Binding Proteins / chemistry*

Substances

  • Capsid Proteins
  • RNA-Binding Proteins
  • RNA

Associated data

  • PDB/5MSF
  • PDB/7MSF