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Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA

Author

Listed:
  • Alfred A. Antson

    (York Structural Biology Laboratory, University of York)

  • Eleanor J. Dodson

    (York Structural Biology Laboratory, University of York)

  • Guy Dodson

    (York Structural Biology Laboratory, University of York)

  • Richard B. Greaves

    (York Structural Biology Laboratory, University of York)

  • Xiao-ping Chen

    (State University of New York
    CuraGen Corp.)

  • Paul Gollnick

    (State University of New York)

Abstract

The trp RNA-binding attenuation protein (TRAP) regulates expression of the tryptophan biosynthetic genes of several bacilli by binding single-stranded RNA. The binding sequence is composed of eleven triplet repeats, predominantly GAG, separated by two or three non-conserved nucleotides. Here we present the crystal structure of a complex of TRAP and a 53-base single-stranded RNA containing eleven GAG triplets, revealing that each triplet is accommodated in a binding pocket formed by β-strands. In the complex, the RNA has an extended structure without any base-pairing and binds to the protein mostly by specific protein–base interactions. Eleven binding pockets on the circular TRAP 11-mer form a belt with a diameter of about 80 Å. This simple but elegant mechanism of arresting the RNA segment by encircling it around a protein disk is applicable to both transcription, when TRAP binds the nascent RNA, and to translation, when TRAP binds the same sequence within a non-coding leader region of the messenger RNA.

Suggested Citation

  • Alfred A. Antson & Eleanor J. Dodson & Guy Dodson & Richard B. Greaves & Xiao-ping Chen & Paul Gollnick, 1999. "Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA," Nature, Nature, vol. 401(6750), pages 235-242, September.
    • Handle: RePEc:nat:nature:v:401:y:1999:i:6750:d:10.1038_45730
    DOI: 10.1038/45730
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