PMID:10625422
| Citation |
Foster, PG, Huang, L, Santi, DV and Stroud, RM (2000) The structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I. Nat. Struct. Biol. 7:23-7 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1038/71219 |
| Keywords |
Amino Acid Sequence; Anticodon/genetics; Anticodon/metabolism; Aspartic Acid/metabolism; Binding Sites; Conserved Sequence; Crystallization; Crystallography, X-Ray; Dimerization; Escherichia coli/enzymology; Hydro-Lyases/chemistry; Hydro-Lyases/metabolism; Hydrogen Bonding; Models, Molecular; Molecular Sequence Data; Protein Structure, Secondary; Protein Structure, Tertiary; Pseudouridine/biosynthesis; Pseudouridine/genetics; RNA, Transfer/genetics; RNA, Transfer/metabolism; RNA-Binding Proteins/chemistry; RNA-Binding Proteins/metabolism; Substrate Specificity; Uridine/metabolism |
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