4J9J

Structure of designed HisF

4J9J の概要

• エントリーDOI: 10.2210/pdb4j9j/pdb
• 分子名称: Imidazole glycerol phosphate synthase subunit HisF (2 entities in total)
• 機能のキーワード: beta barrel, protein engineering, lyase
• 由来する生物種: Thermotoga maritima; 詳細
• 細胞内の位置: Cytoplasm: Q9X0C6
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26326.29

構造登録者

Sterner, R.,Rajendran, C.,Sperl, J. (登録日: 2013-02-16, 公開日: 2013-07-17, 最終更新日: 2023-09-20)

主引用文献

Sperl, J.M.,Rohweder, B.,Rajendran, C.,Sterner, R.
Establishing catalytic activity on an artificial ( beta alpha )8-barrel protein designed from identical half-barrels.
Febs Lett., 587:2798-2805, 2013

PubMed Abstract: It has been postulated that the ubiquitous (βα)8-barrel enzyme fold has evolved by duplication and fusion of an ancestral (βα)4-half-barrel. We have previously reconstructed this process in the laboratory by fusing two copies of the C-terminal half-barrel HisF-C of imidazole glycerol phosphate synthase (HisF). The resulting construct HisF-CC was stepwise stabilized to Sym1 and Sym2, which are extremely robust but catalytically inert proteins. Here, we report on the generation of a circular permutant of Sym2 and the establishment of a sugar isomerization reaction on its scaffold. Our results demonstrate that duplication and mutagenesis of (βα)4-half-barrels can readily lead to a stable and catalytically active (βα)8-barrel enzyme.

PubMed: 23806364
DOI: 10.1016/j.febslet.2013.06.022

実験手法

X-RAY DIFFRACTION (2.3 Å)