6o9a

Crystal structure of MqnA complexed with 3-hydroxybenzoic acid

spinqualitylabelsall models 6o9a, resolution 2.33Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6o9a is a 2 chain structure with sequence from Deinococcus radiodurans R1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.326Å Ligands: 3HB, ACT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9RXE3_DEIRA Catalyzes the dehydration of chorismate into 3-[(1-carboxyvinyl)oxy]benzoate, a step in the biosynthesis of menaquinone (MK, vitamin K2).[HAMAP-Rule:MF_00995] Publication Abstract from PubMed 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. Menaquinone Biosynthesis: Biochemical and Structural Studies of Chorismate Dehydratase.,Mahanta N, Hicks KA, Naseem S, Zhang Y, Fedoseyenko D, Ealick SE, Begley TP Biochemistry. 2019 Mar 22. doi: 10.1021/acs.biochem.9b00105. PMID:30855131 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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