3H39

The complex structure of CCA-adding enzyme with ATP

3H39 の概要

• エントリーDOI: 10.2210/pdb3h39/pdb
• 関連するPDBエントリー: 3H37 3H38 3H3A
• 分子名称: TRNA nucleotidyl transferase-related protein, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• 機能のキーワード: transferase/rna, nucleotide-binding, nucleotidyltransferase, rna-binding, transferase
• 由来する生物種: Thermotoga maritima
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 104075.60

構造登録者

Toh, Y.,Tomita, K. (登録日: 2009-04-16, 公開日: 2009-10-13, 最終更新日: 2023-11-01)

主引用文献

Toh, Y.,Takeshita, D.,Numata, T.,Fukai, S.,Nureki, O.,Tomita, K.
Mechanism for the definition of elongation and termination by the class II CCA-adding enzyme
Embo J., 28:3353-3365, 2009

PubMed Abstract: The CCA-adding enzyme synthesizes the CCA sequence at the 3' end of tRNA without a nucleic acid template. The crystal structures of class II Thermotoga maritima CCA-adding enzyme and its complexes with CTP or ATP were determined. The structure-based replacement of both the catalytic heads and nucleobase-interacting neck domains of the phylogenetically closely related Aquifex aeolicus A-adding enzyme by the corresponding domains of the T. maritima CCA-adding enzyme allowed the A-adding enzyme to add CCA in vivo and in vitro. However, the replacement of only the catalytic head domain did not allow the A-adding enzyme to add CCA, and the enzyme exhibited (A, C)-adding activity. We identified the region in the neck domain that prevents (A, C)-adding activity and defines the number of nucleotide incorporations and the specificity for correct CCA addition. We also identified the region in the head domain that defines the terminal A addition after CC addition. The results collectively suggest that, in the class II CCA-adding enzyme, the head and neck domains collaboratively and dynamically define the number of nucleotide additions and the specificity of nucleotide selection.

PubMed: 19745807
DOI: 10.1038/emboj.2009.260

実験手法

X-RAY DIFFRACTION (2.854 Å)