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Structural insights of the MenD from Escherichia coli reveal ThDP affinity
- Authors
- Priyadarshi, Amit; Saleem, Yasar; Nam, Ki Hyun; Kim, Key-Sun; Park, Sam-Yong; Kim, Eunice EunKyeong; Hwang, Kwang Yeon
- Issue Date
- 20-3월-2009
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- Menaquinone; MenD; ThDP; Oxoglutarate; Decarboxylase; Transferase
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.380, no.4, pp.797 - 801
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 380
- Number
- 4
- Start Page
- 797
- End Page
- 801
- ISSN
- 0006-291X
- 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. (C) 2009 Elsevier Inc. All rights reserved.
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