Crystal structure of the RNA-binding domain from transcription termination factor rho

Nat Struct Biol. 1998 May;5(5):352-6. doi: 10.1038/nsb0598-352.

Abstract

Transcription termination factor rho is an ATP-dependent hexameric helicase found in most eubacterial species. The Escherichia coli rho monomer consists of two domains, an RNA-binding domain (residues 1-130) and an ATPase domain (residues 131-419). The ATPase domain is homologous to the beta subunit of F1-ATPase. Here, we report that the crystal structure of the RNA-binding domain of rho (rho130) at 1.55 A confirms that rho130 contains the oligosaccharide/oligonucleotide-binding (OB) fold, a five stranded beta-barrel. The beta-barrel of rho130 is also surprisingly similar to the N-terminal beta-barrel of F1 ATPase, extending the applicability of F1 ATPase as a structural model for hexameric rho.

Publication types

  • Letter
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Crystallography, X-Ray
  • Escherichia coli / chemistry
  • Models, Molecular
  • Protein Folding
  • Protein Structure, Tertiary*
  • Proton-Translocating ATPases / chemistry
  • RNA-Binding Proteins / chemistry*
  • Rho Factor / chemistry*

Substances

  • RNA-Binding Proteins
  • Rho Factor
  • Proton-Translocating ATPases

Associated data

  • PDB/1A62