1R89

Crystal Structures of an Archaeal Class I CCA-Adding Enzyme and Its Nucleotide Complexes

1R89 の概要

• エントリーDOI: 10.2210/pdb1r89/pdb
• 関連するPDBエントリー: 1R8A 1R8B 1R8C
• 分子名称: tRNA nucleotidyltransferase, MANGANESE (II) ION, SODIUM ION, ... (7 entities in total)
• 機能のキーワード: cca adding enzyme, incoming nucleotide, nucleotidyltransferase superfamily, transferase
• 由来する生物種: Archaeoglobus fulgidus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52683.01

構造登録者

Xiong, Y.,Li, F.,Wang, J.,Weiner, A.M.,Steitz, T.A. (登録日: 2003-10-23, 公開日: 2003-12-16, 最終更新日: 2024-02-14)

主引用文献

Xiong, Y.,Li, F.,Wang, J.,Weiner, A.M.,Steitz, T.A.
Crystal structures of an archaeal class I CCA-adding enzyme and its nucleotide complexes
Mol.Cell, 12:1165-1172, 2003

PubMed Abstract: CCA-adding enzymes catalyze the addition of CCA onto the 3' terminus of immature tRNAs without using a nucleic acid template and have been divided into two classes based on their amino acid sequences. We have determined the crystal structures of a class I CCA-adding enzyme from Archeoglobus fulgidus (AfCCA) and its complexes with ATP, CTP, or UTP. Although it and the class II bacterial Bacillus stearothermophilus CCA enzyme (BstCCA) have similar dimensions and domain architectures (head, neck, body, and tail), only the polymerase domain is structurally homologous. Moreover, the relative orientation of the head domain with respect to the body and tail domains, which appear likely to bind tRNA, differs significantly between the two enzyme classes. Unlike the class II BstCCA, this enzyme binds nucleotides nonspecifically in the absence of bound tRNA. The shape and electrostatic charge distribution of the AfCCA enzyme suggests a model for tRNA binding that accounts for the phosphates that are protected from chemical modification by tRNA binding to AfCCA. The structures of the AfCCA enzyme and the eukaryotic poly(A) polymerase are very similar, implying a close evolutionary relationship between them.

PubMed: 14636575
DOI: 10.1016/S1097-2765(03)00440-4

実験手法

X-RAY DIFFRACTION (1.8 Å)