1DJ0

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

1DJ0 の概要

• エントリーDOI: 10.2210/pdb1dj0/pdb
• 分子名称: PSEUDOURIDINE SYNTHASE I, CHLORIDE ION (3 entities in total)
• 機能のキーワード: alpha/beta fold, rna-binding motif, rna-modifying enzyme, lyase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59518.64

構造登録者

Foster, P.G.,Huang, L.,Santi, D.V.,Stroud, R.M. (登録日: 1999-11-30, 公開日: 2000-05-31, 最終更新日: 2024-02-07)

主引用文献

Foster, P.G.,Huang, L.,Santi, D.V.,Stroud, R.M.
The structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I.
Nat.Struct.Biol., 7:23-27, 2000

PubMed 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.

PubMed: 10625422
DOI: 10.1038/71219

実験手法

X-RAY DIFFRACTION (1.5 Å)