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3AQL

Structure of bacterial protein (apo form II)

3AQL の概要
エントリーDOI10.2210/pdb3aql/pdb
関連するPDBエントリー3AQK 3AQM 3AQN
分子名称Poly(A) polymerase, MAGNESIUM ION, GLYCEROL (3 entities in total)
機能のキーワードtransferase/rna, atp-binding, nucleotide-binding, rna-binding, transferase, nucleotidyltransferase, atp binding, a-phosphorylation
由来する生物種Escherichia coli
タンパク質・核酸の鎖数2
化学式量合計96263.02
構造登録者
Toh, Y.,Takeshita, D.,Tomita , K. (登録日: 2010-11-09, 公開日: 2011-02-09, 最終更新日: 2024-03-13)
主引用文献Toh, Y.,Takeshita, D.,Nagaike, T.,Numata, T.,Tomita, K.
Mechanism for the alteration of the substrate specificities of template-independent RNA polymerases
Structure, 19:232-243, 2011
Cited by
PubMed Abstract: PolyA polymerase (PAP) adds a polyA tail onto the 3'-end of RNAs without a nucleic acid template, using adenosine-5'-triphosphate (ATP) as a substrate. The mechanism for the substrate selection by eubacterial PAP remains obscure. Structural and biochemical studies of Escherichia coli PAP (EcPAP) revealed that the shape and size of the nucleobase-interacting pocket of EcPAP are maintained by an intra-molecular hydrogen-network, making it suitable for the accommodation of only ATP, using a single amino acid, Arg(197). The pocket structure is sustained by interactions between the catalytic domain and the RNA-binding domain. EcPAP has a flexible basic C-terminal region that contributes to optimal RNA translocation for processive adenosine 5'-monophosphate (AMP) incorporations onto the 3'-end of RNAs. A comparison of the EcPAP structure with those of other template-independent RNA polymerases suggests that structural changes of domain(s) outside the conserved catalytic core domain altered the substrate specificities of the template-independent RNA polymerases.
PubMed: 21300291
DOI: 10.1016/j.str.2010.12.006
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3 Å)
構造検証レポート
Validation report summary of 3aql
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-08に公開中

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