Structural insights of the MenD from Escherichia coli reveal ThDP affinity

Amit Priyadarshi; Yasar Saleem; Ki Hyun Nam; Key Sun Kim; Sam Yong Park; Eunice Eun Kyeong Kim; Kwang Yeon Hwang

doi:10.1016/j.bbrc.2009.01.168

Structural insights of the MenD from Escherichia coli reveal ThDP affinity

Amit Priyadarshi, Yasar Saleem, Ki Hyun Nam, Key Sun Kim, Sam Yong Park, Eunice Eun Kyeong Kim, Kwang Yeon Hwang

Department of Biosystems and Biotechnology

Research output: Contribution to journal › Article › peer-review

11 Citations (Scopus)

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.

Original language	English
Pages (from-to)	797-801
Number of pages	5
Journal	Biochemical and biophysical research communications
Volume	380
Issue number	4
DOIs	https://doi.org/10.1016/j.bbrc.2009.01.168
Publication status	Published - 2009 Mar 20

Keywords

Decarboxylase
MenD
Menaquinone
Oxoglutarate
ThDP
Transferase

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1016/j.bbrc.2009.01.168

Cite this

@article{2c83088cd7f64d97b241c26af3da1115,

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.",

keywords = "Decarboxylase, MenD, Menaquinone, Oxoglutarate, ThDP, Transferase",

author = "Amit Priyadarshi and Yasar Saleem and Nam, {Ki Hyun} and Kim, {Key Sun} and Park, {Sam Yong} and Kim, {Eunice Eun Kyeong} and Hwang, {Kwang Yeon}",

note = "Funding Information: We thank staff of BL-17A of the Photon factory, Japan for their assistance. In addition, A. Priyadarshi and E.E. Kim were supported by KIST funds. This work was supported by the 21C Functional Proteomics Frontier R & D Program of the Korea Ministry of Science and Technology.",

year = "2009",

month = mar,

day = "20",

doi = "10.1016/j.bbrc.2009.01.168",

language = "English",

volume = "380",

pages = "797--801",

journal = "Biochemical and biophysical research communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "4",

}

TY - JOUR

T1 - Structural insights of the MenD from Escherichia coli reveal ThDP affinity

AU - Priyadarshi, Amit

AU - Saleem, Yasar

AU - Nam, Ki Hyun

AU - Kim, Key Sun

AU - Park, Sam Yong

AU - Kim, Eunice Eun Kyeong

AU - Hwang, Kwang Yeon

N1 - Funding Information: We thank staff of BL-17A of the Photon factory, Japan for their assistance. In addition, A. Priyadarshi and E.E. Kim were supported by KIST funds. This work was supported by the 21C Functional Proteomics Frontier R & D Program of the Korea Ministry of Science and Technology.

PY - 2009/3/20

Y1 - 2009/3/20

N2 - 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.

AB - 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.

KW - Decarboxylase

KW - MenD

KW - Menaquinone

KW - Oxoglutarate

KW - ThDP

KW - Transferase

UR - http://www.scopus.com/inward/record.url?scp=60849134816&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2009.01.168

DO - 10.1016/j.bbrc.2009.01.168

M3 - Article

C2 - 19338755

AN - SCOPUS:60849134816

SN - 0006-291X

VL - 380

SP - 797

EP - 801

JO - Biochemical and biophysical research communications

JF - Biochemical and biophysical research communications

IS - 4

ER -

Structural insights of the MenD from Escherichia coli reveal ThDP affinity

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this