1dj0

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1dj0, resolution 1.50Å

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THE CRYSTAL STRUCTURE OF E. COLI PSEUDOURIDINE SYNTHASE I AT 1.5 ANGSTROM RESOLUTION

Overview

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.

About this Structure

1DJ0 is a Single protein structure of sequence from Escherichia coli with CL as ligand. Active as Pseudouridylate synthase, with EC number 4.2.1.70 Full crystallographic information is available from OCA.

Reference

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

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