6O9A

Crystal structure of MqnA complexed with 3-hydroxybenzoic acid

6O9A の概要

• エントリーDOI: 10.2210/pdb6o9a/pdb
• 分子名称: Chorismate dehydratase, ACETATE ION, 3-HYDROXYBENZOIC ACID, ... (4 entities in total)
• 機能のキーワード: menaquinone biosynthesis, lyase
• 由来する生物種: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 69588.59

構造登録者

Hicks, K.A.,Mahanta, N.,Naseem, S.,Fedoseyenko, D.,Begley, T.P.,Ealick, S.E. (登録日: 2019-03-13, 公開日: 2019-04-03, 最終更新日: 2023-10-11)

主引用文献

Mahanta, N.,Hicks, K.A.,Naseem, S.,Zhang, Y.,Fedoseyenko, D.,Ealick, S.E.,Begley, T.P.
Menaquinone Biosynthesis: Biochemical and Structural Studies of Chorismate Dehydratase.
Biochemistry, 58:1837-1840, 2019

PubMed Abstract: Menaquinone (MK, vitamin K) is a lipid-soluble quinone that participates in the bacterial electron transport chain. In mammalian cells, vitamin K functions as an essential vitamin for the activation of several proteins involved in blood clotting and bone metabolism. MqnA is the first enzyme on the futalosine-dependent pathway to menaquinone and catalyzes the aromatization of chorismate by water loss. Here we report biochemical and structural studies of MqnA. These studies suggest that the dehydration reaction proceeds by a variant of the E1cb mechanism in which deprotonation is slower than water loss and that the enol carboxylate of the substrate is serving as the base.

PubMed: 30855131
DOI: 10.1021/acs.biochem.9b00105

実験手法

X-RAY DIFFRACTION (2.326 Å)