Structural insights of the MenD from Escherichia coli reveal ThDP affinity

  • Priyadarshi, Amit; 
  • Saleem, Yasar; 
  • Nam, Ki Hyun; 
  • Kim, Key-Sun; 
  • Park, Sam-Yong; 
  • ... Hwang, Kwang Yeon; 
  • 외 1명
Citations

WEB OF SCIENCE

13
Citations

SCOPUS

15

초록

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.

키워드

Menaquinone; MenD; ThDP; Oxoglutarate; Decarboxylase; Transferase; MENAQUINONE BIOSYNTHESIS; (1R,6R)-2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; IDENTIFICATION; DIPHOSPHATE
제목
Structural insights of the MenD from Escherichia coli reveal ThDP affinity
저자
Priyadarshi, Amit; Saleem, Yasar; Nam, Ki Hyun; Kim, Key-Sun; Park, Sam-Yong; Kim, Eunice EunKyeong; Hwang, Kwang Yeon
DOI
10.1016/j.bbrc.2009.01.168
발행일
2009-03-20
유형
Article
저널명
Biochemical and Biophysical Research Communications
권
380
호
4
페이지
797 ~ 801