Structural insights of the MenD from Escherichia coli reveal ThDP affinity

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

상세 보기

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