1SB7

Crystal structure of the E.coli pseudouridine synthase TruD

1SB7 の概要

• エントリーDOI: 10.2210/pdb1sb7/pdb
• 分子名称: tRNA pseudouridine synthase D, GLYCEROL, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: pseudouridine synthase, 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: 83383.82

構造登録者

Hoang, C.,Ferre-D'Amare, A.R. (登録日: 2004-02-10, 公開日: 2004-06-29, 最終更新日: 2024-10-30)

主引用文献

Hoang, C.,Ferre-D'Amare, A.R.
Crystal structure of the highly divergent pseudouridine synthase TruD reveals a circular permutation of a conserved fold.
Rna, 10:1026-1033, 2004

PubMed Abstract: The pseudouridine (Psi) synthases Pus7p and TruD define a family of RNA-modifying enzymes with no sequence similarity to previously characterized Psi synthases. The 2.2 A resolution structure of Escherichia coli TruD reveals a U-shaped molecule with a catalytic domain that superimposes closely on that of other Psi synthases. A domain that appears to be unique to TruD/Pus7p family enzymes hinges over the catalytic domain, possibly serving to clasp the substrate RNAs. The active site comprises residues that are conserved in other Psi synthases, although at least one comes from a structurally distinct part of the protein. Remarkably, the connectivity of the structural elements of the TruD catalytic domain is a circular permutation of that of its paralogs. Because the sequence of the permuted segment, a beta-strand that bisects the catalytic domain, is conserved among orthologs from bacteria, archaea and eukarya, the permutation likely happened early in evolution.

PubMed: 15208439
DOI: 10.1261/rna.7240504

実験手法

X-RAY DIFFRACTION (2.2 Å)