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The structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I.

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.[1]

References

  1. The structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I. Foster, P.G., Huang, L., Santi, D.V., Stroud, R.M. Nat. Struct. Biol. (2000) [Pubmed]
 
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