2LWY

Solution Structure of Bacterial Intein-Like domain from Clostridium thermocellum

2LWY の概要

• エントリーDOI: 10.2210/pdb2lwy/pdb
• NMR情報: BMRB: 18653
• 分子名称: BACTERIAL INTEIN-LIKE DOMAIN (1 entity in total)
• 機能のキーワード: bil, cthbil4, bacterial intein-like, hint, unknown function
• 由来する生物種: Clostridium thermocellum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15297.48

構造登録者

Aranko, A.S.,Oeemig, J.S.,Iwai, H. (登録日: 2012-08-09, 公開日: 2013-05-08, 最終更新日: 2024-05-15)

主引用文献

Aranko, A.S.,Oeemig, J.S.,Iwai, H.
Structural basis for protein trans-splicing by a bacterial intein-like domain - protein ligation without nucleophilic side chains.
Febs J., 280:3256-3269, 2013

PubMed Abstract: Protein splicing in trans by split inteins has become a useful tool for protein engineering in vivo and in vitro. Inteins require Cys, Ser or Thr at the first residue of the C-terminal flanking sequence because a thiol or hydroxyl group in the side chains is a nucleophile indispensable for the trans-esterification step during protein splicing. Newly-identified distinct sequences with homology to the hedgehog/intein superfamily, called bacterial intein-like (BIL) domains, often do not have Cys, Ser, or Thr as the obligatory nucleophilic residue found in inteins. We demonstrated that BIL domains from Clostridium thermocellum (Cth) are proficient at protein splicing without any sequence changes. We determined the first solution NMR structure of a BIL domain, CthBIL4, to guide engineering of split BIL domains for protein ligation. The newly-engineered split BIL domain could catalyze protein ligation by trans-splicing. Protein ligation without any nucleophilic residues of Cys, Ser and Thr could alleviate junction sequence requirements for protein trans-splicing imposed by split inteins and could broaden applications of protein ligation by protein trans-splicing.

PubMed: 23621571
DOI: 10.1111/febs.12307

実験手法

SOLUTION NMR