3FLM

Crystal structure of menD from E.coli

3FLM の概要

• エントリーDOI: 10.2210/pdb3flm/pdb
• 分子名称: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (2 entities in total)
• 機能のキーワード: menaquinone biosynthesis protein, magnesium, manganese, menaquinone biosynthesis, metal-binding, thiamine pyrophosphate, transferase
• 由来する生物種: Escherichia coli K-12
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 122899.66

構造登録者

Priyadarshi, A.,Hwang, K.Y. (登録日: 2008-12-19, 公開日: 2009-03-24, 最終更新日: 2023-11-01)

主引用文献

Priyadarshi, A.,Saleem, Y.,Nam, K.H.,Kim, K.S.,Park, S.Y.,Kim, E.E.,Hwang, K.Y.
Structural insights of the MenD from Escherichia coli reveal ThDP affinity.
Biochem.Biophys.Res.Commun., 380:797-801, 2009

PubMed Abstract: MenD (2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate) synthase belongs to the superfamily of thiamin diphosphate-dependent decarboxylases, which converts isochorismate and 2-oxoglutarate to SHCHC, pyruvate, and carbon dioxide. Here, we report the first crystal structure of apo-MenD from Escherichia coli determined in tetragonal crystal form. The subunit displays the typical three-domain structure observed for ThDP-dependent enzymes. Analytical gel filtration shows that EcMenD behaves as a dimer as well as a tetramer. Circular dichroism and isothermal calorimetry results confirm EcMenD dependency on ThDP, which concomitantly helps to stabilize with better configuration.

PubMed: 19338755
DOI: 10.1016/j.bbrc.2009.01.168

実験手法

X-RAY DIFFRACTION (2.7 Å)