title: Structural insights of the MenD from Escherichia coli reveal ThDP affinity.
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.
authors.affiliation: Biomedical Research Center, Life Science Division, Korea Institute of Science and Technology, Seongbuk-gu, Seoul 136-791, Republic of Korea.
authors.forename: Amit
authors.initials: A
authors.lastname: Priyadarshi
authors.forename: Yasar
authors.initials: Y
authors.lastname: Saleem
authors.forename: Ki Hyun
authors.initials: KH
authors.lastname: Nam
authors.forename: Key-Sun
authors.initials: KS
authors.lastname: Kim
authors.forename: Sam-Yong
authors.initials: SY
authors.lastname: Park
authors.forename: Eunice EunKyeong
authors.initials: EE
authors.lastname: Kim
authors.forename: Kwang Yeon
authors.initials: KY
authors.lastname: Hwang