Article
The structure of trp RNA-binding attenuation protein.
Nature - 20 Apr 1995
Antson A A, Otridge J, Brzozowski A M, Dodson E J, Dodson G G, Wilson K S, Smith T M, Yang M, Kurecki T, Gollnick P
Abstract excerpt
The crystal structure of the trp RNA-binding attenuation protein of Bacclius subtilis solved at 1.8 A resolution reveals a novel structural arrangement in which the eleven subunits are stabilized through eleven intersubunit beta-sheets to form a beta-wheel with a large central hole. The nature of...
Topics
- Amino Acid Sequence
- Bacillus subtilis
- Bacterial Proteins
- Base Sequence
- Crystallography, X-Ray
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Operon
- Protein Binding
- Protein Conformation
- Protein Structure, Secondary
- RNA, Messenger
- RNA-Binding Proteins
- Sequence Homology, Amino Acid
- Transcription Factors
- Tryptophan