1MIV

Crystal structure of Bacillus stearothermophilus CCA-adding enzyme

1MIV の概要

• エントリーDOI: 10.2210/pdb1miv/pdb
• 関連するPDBエントリー: 1MIW 1MIY
• 分子名称: tRNA CCA-adding enzyme, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: cca-adding enzyme, trna nucleotidyltransferase, translation, transferase
• 由来する生物種: Geobacillus stearothermophilus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 91853.06

構造登録者

Li, F.,Xiong, Y.,Wang, J.,Cho, H.D.,Weiner, A.M.,Steitz, T.A. (登録日: 2002-08-23, 公開日: 2002-12-13, 最終更新日: 2024-11-20)

主引用文献

Li, F.,Xiong, Y.,Wang, J.,Cho, H.D.,Tomita, K.,Weiner, A.M.,Steitz, T.A.
Crystal structures of the Bacillus stearothermophilus CCA-adding enzyme and its complexes with ATP or CTP
Cell(Cambridge,Mass.), 111:815-824, 2002

PubMed Abstract: CCA-adding enzymes polymerize CCA onto the 3' terminus of immature tRNAs without using a nucleic acid template. The 3.0 A resolution crystal structures of the CCA-adding enzyme from Bacillus stearothermophilus and its complexes with ATP or CTP reveal a seahorse-shaped subunit consisting of four domains: head, neck, body, and tail. The head is structurally homologous to the palm domain of DNA polymerase beta but has additional structural features and functions. The neck, body, and tail represent new protein folding motifs. The neck provides a specific template for the incoming ATP or CTP, whereas the body and tail may bind tRNA. Each subunit has one active site capable of switching its base specificity between ATP and CTP, an important component of the CCA-adding mechanism.

PubMed: 12526808
DOI: 10.1016/S0092-8674(02)01115-7

実験手法

X-RAY DIFFRACTION (3.5 Å)