3BMZ

Violacein biosynthetic enzyme VioE

3BMZ の概要

• エントリーDOI: 10.2210/pdb3bmz/pdb
• 分子名称: Putative uncharacterized protein, TETRAETHYLENE GLYCOL, TRIETHYLENE GLYCOL, ... (4 entities in total)
• 機能のキーワード: violacein, biosynthetic protein
• 由来する生物種: Chromobacterium violaceum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46097.65

構造登録者

Ryan, K.S.,Drennan, C.L. (登録日: 2007-12-13, 公開日: 2008-01-01, 最終更新日: 2024-02-21)

主引用文献

Ryan, K.S.,Balibar, C.J.,Turo, K.E.,Walsh, C.T.,Drennan, C.L.
The Violacein Biosynthetic Enzyme VioE Shares a Fold with Lipoprotein Transporter Proteins
J.Biol.Chem., 283:6467-6475, 2008

PubMed Abstract: VioE, an unusual enzyme with no characterized homologues, plays a key role in the biosynthesis of violacein, a purple pigment with antibacterial and cytotoxic properties. Without bound cofactors or metals, VioE, from the bacterium Chromobacterium violaceum, mediates a 1,2 shift of an indole ring and oxidative chemistry to generate prodeoxyviolacein, a precursor to violacein. Our 1.21 A resolution structure of VioE shows that the enzyme shares a core fold previously described for lipoprotein transporter proteins LolA and LolB. For both LolB and VioE, a bound polyethylene glycol molecule suggests the location of the binding and/or active site of the protein. Mutations of residues near the bound polyethylene glycol molecule in VioE have identified the active site and five residues important for binding or catalysis. This structural and mutagenesis study suggests that VioE acts as a catalytic chaperone, using a fold previously associated with lipoprotein transporters to catalyze the production of its prodeoxyviolacein product.

PubMed: 18171675
DOI: 10.1074/jbc.M708573200

実験手法

X-RAY DIFFRACTION (1.21 Å)