4OD4

Apo structure of a UbiA homolog from Aeropyrum pernix K1

4OD4 の概要

• エントリーDOI: 10.2210/pdb4od4/pdb
• 関連するPDBエントリー: 4OD5
• 分子名称: 4-hydroxybenzoate octaprenyltransferase (1 entity in total)
• 機能のキーワード: all alpha helical, intramembrane aromatic prenyltransferase, membrane, transferase
• 由来する生物種: Aeropyrum pernix
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 191018.77

構造登録者

Li, W.,Cheng, W. (登録日: 2014-01-09, 公開日: 2014-03-19, 最終更新日: 2024-02-28)

主引用文献

Cheng, W.,Li, W.
Structural insights into ubiquinone biosynthesis in membranes.
Science, 343:878-881, 2014

PubMed Abstract: Biosynthesis of ubiquinones requires the intramembrane UbiA enzyme, an archetypal member of a superfamily of prenyltransferases that generates lipophilic aromatic compounds. Mutations in eukaryotic superfamily members have been linked to cardiovascular degeneration and Parkinson's disease. To understand how quinones are produced within membranes, we report the crystal structures of an archaeal UbiA in its apo and substrate-bound states at 3.3 and 3.6 angstrom resolution, respectively. The structures reveal nine transmembrane helices and an extramembrane cap domain that surround a large central cavity containing the active site. To facilitate the catalysis inside membranes, UbiA has an unusual active site that opens laterally to the lipid bilayer. Our studies illuminate general mechanisms for substrate recognition and catalysis in the UbiA superfamily and rationalize disease-related mutations in humans.

PubMed: 24558159
DOI: 10.1126/science.1246774

実験手法

X-RAY DIFFRACTION (3.301 Å)