3AQL
Structure of bacterial protein (apo form II)
3AQL の概要
| エントリーDOI | 10.2210/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 | |
| 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: 21300291DOI: 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) |
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