title: NMR structure of the bacteriophage lambda N peptide/boxB RNA complex: recognition of a GNRA fold by an arginine-rich motif.
abstract: The structure of the complex formed by the arginine-rich motif of the transcriptional antitermination protein N of phage lambda and boxB RNA was determined by heteronuclear magnetic resonance spectroscopy. A bent alpha helix in N recognizes primarily the shape and negatively charged surface of the boxB hairpin through multiple hydrophobic and ionic interactions. The GAAGA boxB loop forms a GNRA fold, previously described for tetraloops, which is essential for N binding. The fourth nucleotide of the loop extrudes from the GNRA fold to enable the E. coli elongation factor NusA to recognize the N protein/RNA complex. This structure reveals a new mode of RNA-protein recognition and shows how a small RNA element can facilitate a protein-protein interaction and thereby nucleate formation of a large ribonucleoprotein complex.
authors.affiliation: Banting and Best Department of Medical Research, University of Toronto, Ontario, Canada.
authors.forename: P
authors.initials: P
authors.lastname: Legault
authors.forename: J
authors.initials: J
authors.lastname: Li
authors.forename: J
authors.initials: J
authors.lastname: Mogridge
authors.forename: L E
authors.initials: LE
authors.lastname: Kay
authors.forename: J
authors.initials: J
authors.lastname: Greenblatt
mesh_terms: D000595:Amino Acid Sequence; D001120:Arginine / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D010582:Bacteriophage lambda / Q000737:chemistry*; D004926:Escherichia coli; D029968:Escherichia coli Proteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D009690:Nucleic Acid Conformation; D010445:Peptide Elongation Factors; D017433:Protein Structure, Secondary; D012367:RNA, Viral / Q000737:chemistry* / Q000378:metabolism; D012261:Ribonucleoproteins / Q000737:chemistry; D014157:Transcription Factors / Q000737:chemistry / Q000378:metabolism; D035602:Transcriptional Elongation Factors; D054334:Viral Regulatory and Accessory Proteins / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C059417:N protein, Bacteriophage lambda; D010445:Peptide Elongation Factors; D012367:RNA, Viral; D012261:Ribonucleoproteins; D014157:Transcription Factors; D035602:Transcriptional Elongation Factors; D054334:Viral Regulatory and Accessory Proteins; C068727:nusA protein, E coli; D001120:Arginine