6RPQ

Crystal structure of PhoCDC21-1 intein

6RPQ の概要

• エントリーDOI: 10.2210/pdb6rpq/pdb
• 分子名称: Ubiquitin-like protein SMT3,1108aa long hypothetical cell division control protein (1 entity in total)
• 機能のキーワード: intein, protein-splicing, hint, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32263.50

構造登録者

Beyer, H.M.,Mikula, K.M.,Iwai, H. (登録日: 2019-05-14, 公開日: 2019-08-14, 最終更新日: 2024-01-24)

主引用文献

Beyer, H.M.,Mikula, K.M.,Kudling, T.V.,Iwai, H.
Crystal structures of CDC21-1 inteins from hyperthermophilic archaea reveal the selection mechanism for the highly conserved homing endonuclease insertion site.
Extremophiles, 23:669-679, 2019

PubMed Abstract: Self-splicing inteins are mobile genetic elements invading host genes via nested homing endonuclease (HEN) domains. All HEN domains residing within inteins are inserted at a highly conserved insertion site. A purifying selection mechanism directing the location of the HEN insertion site has not yet been identified. In this work, we solved the three-dimensional crystal structures of two inteins inserted in the cell division control protein 21 of the hyperthermophilic archaea Pyrococcus abyssi and Pyrococcus horikoshii. A comparison between the structures provides the structural basis for the thermo-stabilization mechanism of inteins that have lost the HEN domain during evolution. The presence of an entire extein domain in the intein structure from Pyrococcus horikoshii suggests the selection mechanism for the highly conserved HEN insertion point.

PubMed: 31363851
DOI: 10.1007/s00792-019-01117-4

実験手法

X-RAY DIFFRACTION (2.654 Å)