Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
, 401 (6750), 235-42

Structure of the Trp RNA-binding Attenuation Protein, TRAP, Bound to RNA

Affiliations

Structure of the Trp RNA-binding Attenuation Protein, TRAP, Bound to RNA

A A Antson et al. Nature.

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 beta-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 A. 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.

Similar articles

See all similar articles

Cited by 76 articles

See all "Cited by" articles

Publication types

MeSH terms

LinkOut - more resources

Feedback