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