4HU9

E. coli thioredoxin variant with (4S)-FluoroPro76 as single proline residue

4HU9 の概要

• エントリーDOI: 10.2210/pdb4hu9/pdb
• 関連するPDBエントリー: 4HU7 4HUA
• 分子名称: Thioredoxin-1, COPPER (II) ION (3 entities in total)
• 機能のキーワード: 4s-fluoroproline, cisproline, thioredoxin fold, protein disulfide oxidoreductase activity, oxidoreductase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11664.77

構造登録者

Scharer, M.A.,Rubini, M.,Capitani, G.,Glockshuber, R. (登録日: 2012-11-02, 公開日: 2013-05-29, 最終更新日: 2017-09-20)

主引用文献

Rubini, M.,Scharer, M.A.,Capitani, G.,Glockshuber, R.
(4R)- and (4S)-Fluoroproline in the Conserved cis-Prolyl Peptide Bond of the Thioredoxin Fold: Tertiary Structure Context Dictates Ring Puckering.
Chembiochem, 14:1053-1057, 2013

PubMed Abstract: Fine-tuning protein stability: The non-natural amino acids (2S,4R)- and (2S,4S)-fluoroproline modulate protein stability by biasing the proline ring pucker and the cis/trans equilibrium of prolyl peptide bonds. We incorporated both fluoroproline stereoisomers at the invariant cis-proline residue of the thioredoxin fold. The results show that tertiary structure context overrules the conformational preferences of fluoroprolines.

PubMed: 23712956
DOI: 10.1002/cbic.201300178

実験手法

X-RAY DIFFRACTION (1.55 Å)