5ONN

Crystal Structure of Ectoine Synthase from P. lautus

5ONN の概要

• エントリーDOI: 10.2210/pdb5onn/pdb
• 関連するPDBエントリー: 5ONM
• 分子名称: L-ectoine synthase, FE (III) ION, (2~{S})-4-acetamido-2-azanyl-butanoic acid, ... (4 entities in total)
• 機能のキーワード: ectoine, synthase, osmolyte, metal binding protein
• 由来する生物種: Paenibacillus lautus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15756.59

構造登録者

Bremer, E. (登録日: 2017-08-04, 公開日: 2018-08-22, 最終更新日: 2024-01-17)

主引用文献

Czech, L.,Hoppner, A.,Kobus, S.,Seubert, A.,Riclea, R.,Dickschat, J.S.,Heider, J.,Smits, S.H.J.,Bremer, E.
Illuminating the catalytic core of ectoine synthase through structural and biochemical analysis.
Sci Rep, 9:364-364, 2019

PubMed Abstract: Ectoine synthase (EctC) is the signature enzyme for the production of ectoine, a compatible solute and chemical chaperone widely synthesized by bacteria as a cellular defense against the detrimental effects of osmotic stress. EctC catalyzes the last step in ectoine synthesis through cyclo-condensation of the EctA-formed substrate N-gamma-acetyl-L-2,4-diaminobutyric acid via a water elimination reaction. We have biochemically and structurally characterized the EctC enzyme from the thermo-tolerant bacterium Paenibacillus lautus (Pl). EctC is a member of the cupin superfamily and forms dimers, both in solution and in crystals. We obtained high-resolution crystal structures of the (Pl)EctC protein in forms that contain (i) the catalytically important iron, (ii) iron and the substrate N-gamma-acetyl-L-2,4-diaminobutyric acid, and (iii) iron and the enzyme reaction product ectoine. These crystal structures lay the framework for a proposal for the EctC-mediated water-elimination reaction mechanism. Residues involved in coordinating the metal, the substrate, or the product within the active site of ectoine synthase are highly conserved among a large group of EctC-type proteins. Collectively, the biochemical, mutational, and structural data reported here yielded detailed insight into the structure-function relationship of the (Pl)EctC enzyme and are relevant for a deeper understanding of the ectoine synthase family as a whole.

PubMed: 30674920
DOI: 10.1038/s41598-018-36247-w

実験手法

X-RAY DIFFRACTION (1.4 Å)