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

Alfred A. Antson (), Eleanor J. Dodson, Guy Dodson, Richard B. Greaves, Xiao-ping Chen and Paul Gollnick
Additional contact information
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
Paul Gollnick: State University of New York

Nature, 1999, vol. 401, issue 6750, 235-242

Abstract: 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.

Date: 1999
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/45730 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:401:y:1999:i:6750:d:10.1038_45730

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/45730

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().