6O9A

Crystal structure of MqnA complexed with 3-hydroxybenzoic acid

Summary for 6O9A

• Entry DOI: 10.2210/pdb6o9a/pdb
• Descriptor: Chorismate dehydratase, ACETATE ION, 3-HYDROXYBENZOIC ACID, ... (4 entities in total)
• Functional Keywords: menaquinone biosynthesis, lyase
• Biological source: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
• Total number of polymer chains: 2
• Total formula weight: 69588.59

Authors

Hicks, K.A.,Mahanta, N.,Naseem, S.,Fedoseyenko, D.,Begley, T.P.,Ealick, S.E. (deposition date: 2019-03-13, release date: 2019-04-03, Last modification date: 2023-10-11)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.326 Å)