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2N68

Solution study of Astexin1

2N68 の概要
エントリーDOI10.2210/pdb2n68/pdb
NMR情報BMRB: 25754
分子名称astexin1 (1 entity in total)
機能のキーワードunknown function
由来する生物種Asticcacaulis excentricus CB 48
タンパク質・核酸の鎖数1
化学式量合計2583.70
構造登録者
Link, A.J.,Maksimov, M.O. (登録日: 2015-08-13, 公開日: 2015-11-04, 最終更新日: 2024-05-15)
主引用文献Zong, C.,Maksimov, M.O.,Link, A.J.
Construction of Lasso Peptide Fusion Proteins.
Acs Chem.Biol., 11:61-68, 2016
Cited by
PubMed Abstract: Lasso peptides are a family of ribosomally synthesized and post-translationally modified peptides (RiPPs) typified by an isopeptide-bonded macrocycle between the peptide N-terminus and an aspartate or glutamate side chain. The C-terminal portion of the peptide threads through the N-terminal macrocycle to give the characteristic lasso fold. Because of the inherent stability, both proteolytic and often thermal, of lasso peptides, we became interested in whether proteins could be fused to the free C-terminus of lasso peptides. Here, we demonstrate fusion of two model proteins, the artificial leucine zipper A1 and the superfolder variant of GFP, to the C-terminus of the lasso peptide astexin-1. Successful lasso cyclization of the N-terminus of these fusion proteins requires a flexible linker in between the C-terminus of the lasso peptide and the N-terminus of the protein of interest. The ability to fuse lasso peptides to a protein of interest is an important step toward phage and bacterial display systems for the high-throughput screening of lasso peptide libraries for new functions.
PubMed: 26492187
DOI: 10.1021/acschembio.5b00745
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 2n68
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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