title: The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold.
abstract: The S1 domain, originally identified in ribosomal protein S1, is found in a large number of RNA-associated proteins. The structure of the S1 RNA-binding domain from the E. coli polynucleotide phosphorylase has been determined using NMR methods and consists of a five-stranded antiparallel beta barrel. Conserved residues on one face of the barrel and adjacent loops form the putative RNA-binding site. The structure of the S1 domain is very similar to that of cold shock protein, suggesting that they are both derived from an ancient nucleic acid-binding protein. Enhanced sequence searches reveal hitherto unidentified S1 domains in RNase E, RNase II, NusA, EMB-5, and other proteins.
authors.affiliation: Department of Chemistry, University of Cambridge, United Kingdom.
authors.forename: M
authors.initials: M
authors.lastname: Bycroft
authors.forename: T J
authors.initials: TJ
authors.lastname: Hubbard
authors.forename: M
authors.initials: M
authors.lastname: Proctor
authors.forename: S M
authors.initials: SM
authors.lastname: Freund
authors.forename: A G
authors.initials: AG
authors.lastname: Murzin
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D003080:Cold Temperature; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology; D015852:Eukaryotic Initiation Factor-2 / Q000378:metabolism; D005656:Fungal Proteins / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011117:Polyribonucleotide Nucleotidyltransferase / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012313:RNA / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D012269:Ribosomal Proteins / Q000737:chemistry; D019892:eIF-2 Kinase
chemical_list: D001426:Bacterial Proteins; D015852:Eukaryotic Initiation Factor-2; D005656:Fungal Proteins; D016601:RNA-Binding Proteins; D012269:Ribosomal Proteins; C015494:ribosomal protein S1; D012313:RNA; D017346:Protein Serine-Threonine Kinases; D019892:eIF-2 Kinase; D011117:Polyribonucleotide Nucleotidyltransferase