3HWX

Crystal structure of menaquinone synthesis protein MenD from E. coli in complex with ThDP

3HWX の概要

• エントリーDOI: 10.2210/pdb3hwx/pdb
• 関連するPDBエントリー: 3FLM
• 分子名称: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase, SODIUM ION, THIAMINE DIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: menaquinone, thdp, mg, vitamin k2, carboxylase, magnesium, manganese, menaquinone biosynthesis, metal-binding, thiamine pyrophosphate, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 495724.61

構造登録者

Priyadarshi, A.,Hwang, K.Y. (登録日: 2009-06-19, 公開日: 2009-11-03, 最終更新日: 2023-11-01)

主引用文献

Priyadarshi, A.,Kim, E.E.,Hwang, K.Y.
Structural and functional analysis of Vitamin K2 synthesis protein MenD.
Biochem.Biophys.Res.Commun., 388:748-751, 2009

PubMed Abstract: Here we describe in detail the crystal structures of the Vitamin K(2) synthesis protein MenD, from Escherichia coli, in complex with thiamine diphosphate (ThDP) and oxoglutarate, and the effects of cofactor and substrate on its structural stability. This is the first reported structure of MenD in complex with oxoglutarate. The residues Gly472 to Phe488 of the active site region are either disordered, or in an open conformation in the MenD oxoglutarate complex structure, but adopt a closed conformation in the MenD ThDP complex structure. Biospecific-interaction analysis using surface plasmon resonance (SPR) technology reveals an affinity for ThDP and oxoglutarate in the nanomolar range. Biochemical and structural analysis confirmed that MenD is highly dependent on ThDP for its structural stability. Our structural results combined with the biochemical assay reveal novel features of the enzyme that could be utilized in a program of rational structure-based drug design, as well as in helping to enhance our knowledge of the menaquinone synthesis pathway in greater detail.

PubMed: 19703421
DOI: 10.1016/j.bbrc.2009.08.093

実験手法

X-RAY DIFFRACTION (2.6 Å)