title: The structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I.
abstract: Pseudouridine synthases catalyze the isomerization of specific uridines to pseudouridine in a variety of RNAs, yet the basis for recognition of the RNA sites or how they catalyze this reaction is unknown. The crystal structure of pseudouridine synthase I from Escherichia coli, which, for example, modifies positions 38, 39 and/or 40 in tRNA, reveals a dimeric protein that contains two positively charged, RNA-binding clefts along the surface of the protein. Each cleft contains a highly conserved aspartic acid located at its center. The structural domains have a topological similarity to those of other RNA-binding proteins, though the mode of interaction with tRNA appears to be unique. The structure suggests that a dimeric enzyme is required for binding transfer RNA and subsequent pseudouridine formation.
authors.affiliation: Department of Biochemistry and Biophysics, University of California San Francisco, San Francisco, California 94143-0448, USA.
authors.forename: P G
authors.initials: PG
authors.lastname: Foster
authors.forename: L
authors.initials: L
authors.lastname: Huang
authors.forename: D V
authors.initials: DV
authors.lastname: Santi
authors.forename: R M
authors.initials: RM
authors.lastname: Stroud
mesh_terms: D000595:Amino Acid Sequence; D000926:Anticodon / Q000235:genetics / Q000378:metabolism; D001224:Aspartic Acid / Q000378:metabolism; D001665:Binding Sites; D017124:Conserved Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D019281:Dimerization; D004926:Escherichia coli / Q000201:enzymology*; D006836:Hydro-Lyases / Q000737:chemistry* / Q000378:metabolism*; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011560:Pseudouridine / Q000096:biosynthesis* / Q000235:genetics; D012343:RNA, Transfer / Q000235:genetics / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity; D014529:Uridine / Q000378:metabolism
chemical_list: D000926:Anticodon; D016601:RNA-Binding Proteins; D011560:Pseudouridine; D001224:Aspartic Acid; D012343:RNA, Transfer; D006836:Hydro-Lyases; C022479:pseudouridylate synthetase; D014529:Uridine