Structural highlights
Function
[TRUA_ECOLI] Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hur S, Stroud RM. How U38, 39, and 40 of many tRNAs become the targets for pseudouridylation by TruA. Mol Cell. 2007 Apr 27;26(2):189-203. PMID:17466622 doi:10.1016/j.molcel.2007.02.027
- ↑ Foster PG, Huang L, Santi DV, Stroud RM. The structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I. Nat Struct Biol. 2000 Jan;7(1):23-7. PMID:10625422 doi:10.1038/71219
