title: RNA-protein complexes.
abstract: The three commonly found RNA-binding domains, the ribonucleoprotein (RNP) domain, the double stranded RNA binding domain (dsRBD) and the K homology (KH) domain, have now been shown to have an alpha/beta fold similar to that found in many ribosomal proteins. Crystal structures of two hairpin RNA-protein complexes have been determined recently: the U1A spliceosomal protein bound to hairpin II of U1 small nuclear RNA, and MS2 bacteriophage capsid protein bound to a hairpin present at the ribosomal binding site of MS2 replicase mRNA. The crystal structure of the tryptophan operon RNA binding attenuation protein from Bacillus subtilis shows a novel structure with 11 monomers arranged in a doughnut-shaped ring that binds 11 copies of (U/G)AG triplets presented in the leader sequence of the tryptophan operon polycistronic message.
authors.affiliation: MRC Laboratory of Molecular Biology, Cambridge, UK.
authors.forename: K
authors.initials: K
authors.lastname: Nagai
mesh_terms: D000818:Animals; D001412:Bacillus subtilis / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism; D001665:Binding Sites; D002213:Capsid / Q000378:metabolism; D036022:Capsid Proteins; D017909:Levivirus / Q000378:metabolism; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D011506:Proteins / Q000378:metabolism*; D012313:RNA / Q000378:metabolism*; D012329:RNA, Bacterial / Q000378:metabolism; D012367:RNA, Viral / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000378:metabolism; D017412:Ribonucleoprotein, U1 Small Nuclear / Q000378:metabolism; D017381:Spliceosomes; D014157:Transcription Factors / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D036022:Capsid Proteins; C079092:MtrB protein, Bacteria; D011506:Proteins; D012329:RNA, Bacterial; D012367:RNA, Viral; D016601:RNA-Binding Proteins; D017412:Ribonucleoprotein, U1 Small Nuclear; D014157:Transcription Factors; C075339:U1A protein; D012313:RNA