3FI0

Crystal Structure Analysis of B. stearothermophilus Tryptophanyl-tRNA Synthetase Complexed with Tryptophan, AMP, and Inorganic Phosphate

3FI0 の概要

• エントリーDOI: 10.2210/pdb3fi0/pdb
• 関連するPDBエントリー: 1D2R 1I6K 1I6L 1I6M 1M83 1MAU 1MAW 1MB2 2OV4 3FHJ
• 分子名称: Tryptophanyl-tRNA synthetase, TRYPTOPHAN, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: domain rearrangement, aminoacyl-trna synthetase, atp-binding, cytoplasm, ligase, nucleotide-binding, protein biosynthesis, translation
• 由来する生物種: Bacillus stearothermophilus
• 細胞内の位置: Cytoplasm: P00953
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 684479.59

構造登録者

Laowanapiban, P.,Kapustina, M.,Vonrhein, C.,Delarue, M.,Koehl, P.,Carter Jr., C.W. (登録日: 2008-12-10, 公開日: 2009-02-03, 最終更新日: 2024-11-20)

主引用文献

Laowanapiban, P.,Kapustina, M.,Vonrhein, C.,Delarue, M.,Koehl, P.,Carter, C.W.
Independent saturation of three TrpRS subsites generates a partially assembled state similar to those observed in molecular simulations.
Proc.Natl.Acad.Sci.Usa, 106:1790-1795, 2009

PubMed Abstract: Two new crystal structures of Bacillus stearothermophilus tryptophanyl-tRNA synthetase (TrpRS) afford evidence that a closed interdomain hinge angle requires a covalent bond between AMP and an occupant of either pyrophosphate or tryptophan subsite. They also are within experimental error of a cluster of structures observed in a nonequilibrium molecular dynamics simulation showing partial active-site assembly. Further, the highest energy structure in a minimum action pathway computed by using elastic network models for Open and Pretransition state (PreTS) conformations for the fully liganded TrpRS monomer is intermediate between that simulated structure and a partially disassembled structure from a nonequilibrium molecular dynamics trajectory for the unliganded PreTS. These mutual consistencies provide unexpected validation of inferences drawn from molecular simulations.

PubMed: 19174517
DOI: 10.1073/pnas.0812752106

実験手法

X-RAY DIFFRACTION (2.7 Å)