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

Nature Structural Biology volume 5, pages 352–356 (1998)Cite this article

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 β subunit of F1-ATPase. Here, we report that the crystal structure of the RNA-binding domain of rho (rho130) at 1.55 Å confirms that rho130 contains the oligosaccharide/oligonucleotide-binding (OB) fold, a five stranded β-barrel. The β-barrel of rho!30 is also surprisingly similiar to the N-terminal β-barrel of Fl ATPase, extending the applicability of Fl ATPase as a structural model for hexameric rho.

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Authors and Affiliations

  1. Department of Biochemistry, University of Virginia School of Medicine, Charlottesville, Virginia, 22908, USA

    Timothy J. Allison, Todd C. Wood, Deborah M. Briercheck & Gordon S. Rule

  2. Department of Pharmacology, University of Virginia School of Medicine, Charlottesville, Virginia, 22908

    Fraydoon Rastinejad

  3. Department of Chemistry, Indiana University, Bloomington, Indiana, 47405, USA

    John P. Richardson

  4. Department of Biological Sciences, Carnegie Mellon University, 4400 Fifth Avenue, Pittsburgh, Pennsylvania, 15213, USA

    Gordon S. Rule

Authors
  1. Timothy J. Allison
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  3. Deborah M. Briercheck
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  4. Fraydoon Rastinejad
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  6. Gordon S. Rule
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Correspondence to Gordon S. Rule.

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Allison, T., Wood, T., Briercheck, D. et al. Crystal structure of the RNA-binding domain from transcription termination factor rho. Nat Struct Mol Biol 5, 352–356 (1998). https://doi.org/10.1038/nsb0598-352

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