1VS3

Crystal Structure of the tRNA Pseudouridine Synthase TruA From Thermus thermophilus HB8

1VS3 の概要

• エントリーDOI: 10.2210/pdb1vs3/pdb
• 分子名称: tRNA pseudouridine synthase A (2 entities in total)
• 機能のキーワード: trua, pseudouridine synthase, trna modification, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, isomerase
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55506.54

構造登録者

Dong, X.,Bessho, Y.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2006-06-28, 公開日: 2006-12-12, 最終更新日: 2023-12-27)

主引用文献

Dong, X.,Bessho, Y.,Shibata, R.,Nishimoto, M.,Shirouzu, M.,Kuramitsu, S.,Yokoyama, S.
Crystal structure of tRNA pseudouridine synthase TruA from Thermus thermophilus HB8.
Rna Biol., 3:115-122, 2006

PubMed Abstract: The pseudouridine synthase (Psi synthase) TruA catalyzes the conversion of uridine to pseudouridine at positions 38, 39 and/or 40 in the anticodon stem-loop (ASL) of tRNA. We have determined the crystal structure of TruA from Thermus thermophilus HB8 at 2.25 A resolution. TruA and the other (Psi synthases have a completely conserved active site aspartate, which suggests that the members of this enzyme family share a common catalytic mechanism. The T. thermophilus TruA structure reveals the remarkably flexible structural features in the tRNA-binding cleft, which may be responsible for the primary tRNA interaction. In addition, the charged residues occupying the intermediate positions in the cleft may lead the tRNA to the active site for catalysis. Based on the TruB-tRNA complex structure, the T. thermophilus TruA structure reveals that the tRNA probably makes the melting base pairs move into the cleft, and suggests that a conformational change of the substrate tRNA is necessary to facilitate access to the active site aspartate residue, deep within the cleft.

PubMed: 17114947
DOI: 10.4161/rna.3.3.3286

実験手法

X-RAY DIFFRACTION (2.25 Å)