4KL5

Crystal structure of NpuDnaE intein

4KL5 の概要

• エントリーDOI: 10.2210/pdb4kl5/pdb
• 関連するPDBエントリー: 2KEQ
• 分子名称: DNA polymerase III, alpha subunit, Nucleic acid binding, OB-fold, tRNA/helicase-type chimeric construct, CITRIC ACID, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: hint, intein, npudnae inten, unknown function
• 由来する生物種: Nostoc punctiforme; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 33231.09

構造登録者

Aranko, A.S.,Oeemig, J.S.,Kajander, T.,Iwai, H. (登録日: 2013-05-07, 公開日: 2013-09-04, 最終更新日: 2023-09-20)

主引用文献

Aranko, A.S.,Oeemig, J.S.,Kajander, T.,Iwai, H.
Intermolecular domain swapping induces intein-mediated protein alternative splicing.
Nat.Chem.Biol., 9:616-622, 2013

PubMed Abstract: Protein sequences are diversified on the DNA level by recombination and mutation and can be further increased on the RNA level by alternative RNA splicing, involving introns that have important roles in many biological processes. The protein version of introns (inteins), which catalyze protein splicing, were first reported in the 1990s. The biological roles of protein splicing still remain elusive because inteins neither provide any clear benefits nor have an essential role in their host organisms. We now report protein alternative splicing, in which new protein sequences can be produced by protein recombination by intermolecular domain swapping of inteins, as elucidated by NMR spectroscopy and crystal structures. We demonstrate that intein-mediated protein alternative splicing could be a new strategy to increase protein diversity (that is, functions) without any modification in genetic backgrounds. We also exploited it as a post-translational protein conformation-driven switch of protein functions (for example, as highly specific protein interference).

PubMed: 23974115
DOI: 10.1038/nchembio.1320

実験手法

X-RAY DIFFRACTION (1.72 Å)