4K22

Structure of the C-terminal truncated form of E.Coli C5-hydroxylase UBII involved in ubiquinone (Q8) biosynthesis

4K22 の概要

• エントリーDOI: 10.2210/pdb4k22/pdb
• 分子名称: Protein VisC, GLYCEROL, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: rossmann fold, hydroxylase, oxidoreductase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 81610.30

構造登録者

Pecqueur, L.,Lombard, M.,Golinelli-pimpaneau, B.,Fontecave, M. (登録日: 2013-04-07, 公開日: 2013-05-29, 最終更新日: 2024-03-20)

主引用文献

Chehade, M.H.,Loiseau, L.,Lombard, M.,Pecqueur, L.,Ismail, A.,Smadja, M.,Golinelli-Pimpaneau, B.,Mellot-Draznieks, C.,Hamelin, O.,Aussel, L.,Kieffer-Jaquinod, S.,Labessan, N.,Barras, F.,Fontecave, M.,Pierrel, F.
ubiI, a New Gene in Escherichia coli Coenzyme Q Biosynthesis, Is Involved in Aerobic C5-hydroxylation.
J.Biol.Chem., 288:20085-20092, 2013

PubMed Abstract: Coenzyme Q (ubiquinone or Q) is a redox-active lipid found in organisms ranging from bacteria to mammals in which it plays a crucial role in energy-generating processes. Q biosynthesis is a complex pathway that involves multiple proteins. In this work, we show that the uncharacterized conserved visC gene is involved in Q biosynthesis in Escherichia coli, and we have renamed it ubiI. Based on genetic and biochemical experiments, we establish that the UbiI protein functions in the C5-hydroxylation reaction. A strain deficient in ubiI has a low level of Q and accumulates a compound derived from the Q biosynthetic pathway, which we purified and characterized. We also demonstrate that UbiI is only implicated in aerobic Q biosynthesis and that an alternative enzyme catalyzes the C5-hydroxylation reaction in the absence of oxygen. We have solved the crystal structure of a truncated form of UbiI. This structure shares many features with the canonical FAD-dependent para-hydroxybenzoate hydroxylase and represents the first structural characterization of a monooxygenase involved in Q biosynthesis. Site-directed mutagenesis confirms that residues of the flavin binding pocket of UbiI are important for activity. With our identification of UbiI, the three monooxygenases necessary for aerobic Q biosynthesis in E. coli are known.

PubMed: 23709220
DOI: 10.1074/jbc.M113.480368

実験手法

X-RAY DIFFRACTION (2 Å)