1dj0

Publication Abstract from PubMed

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.

The structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I.,Foster PG, Huang L, Santi DV, Stroud RM Nat Struct Biol. 2000 Jan;7(1):23-7. PMID:10625422^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.