4TW3

Insights into Substrate and Metal Binding from the Crystal Structure of Cyanobacterial Aldehyde Deformylating Oxygenase with Substrate Bound

4TW3 の概要

• エントリーDOI: 10.2210/pdb4tw3/pdb
• 分子名称: Aldehyde decarbonylase, FE (III) ION, STEARIC ACID, ... (5 entities in total)
• 機能のキーワード: non-heme di-iron protein, hydrocarbon production, alpha-helix, oxidoreductase
• 由来する生物種: Prochlorococcus marinus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25649.92

構造登録者

Buer, B.C.,Paul, B.,Das, D.,Stuckey, J.A.,Marsh, E.N.G. (登録日: 2014-06-29, 公開日: 2014-10-15, 最終更新日: 2023-09-27)

主引用文献

Buer, B.C.,Paul, B.,Das, D.,Stuckey, J.A.,Marsh, E.N.
Insights into substrate and metal binding from the crystal structure of cyanobacterial aldehyde deformylating oxygenase with substrate bound.
Acs Chem.Biol., 9:2584-2593, 2014

PubMed Abstract: The nonheme diiron enzyme cyanobacterial aldehyde deformylating oxygenase, cADO, catalyzes the highly unusual deformylation of aliphatic aldehydes to alkanes and formate. We have determined crystal structures for the enzyme with a long-chain water-soluble aldehyde and medium-chain carboxylic acid bound to the active site. These structures delineate a hydrophobic channel that connects the solvent with the deeply buried active site and reveal a mode of substrate binding that is different from previously determined structures with long-chain fatty acids bound. The structures also identify a water channel leading to the active site that could facilitate the entry of protons required in the reaction. NMR studies examining 1-[(13)C]-octanal binding to cADO indicate that the enzyme binds the aldehyde form rather than the hydrated form. Lastly, the fortuitous cocrystallization of the metal-free form of the protein with aldehyde bound has revealed protein conformation changes that are involved in binding iron.

PubMed: 25222710
DOI: 10.1021/cb500343j

実験手法

X-RAY DIFFRACTION (1.6 Å)