Crystal structure of uncleaved L-aspartate-α-decarboxylase from Mycobacterium tuberculosis

被引：33

作者：

Gopalan, Gayathri

Chopra, Sidharth

Ranganathan, Anand

Swaminathan, Kunchithapadam ^{[1
]}

机构：

[1] Natl Univ Singapore, Dept Sci Biol, Singapore 117543, Singapore

[2] Int Ctr Genet Engn & Biotechnol, Recombinant Gene Prod Grp, New Delhi 110067, India

[3] Inst Mol & Cell Biol, Singapore 138673, Singapore

来源：

PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 2006年 / 65卷 / 04期

关键词：

crystal structure; Mycobacterium tuberculosis; L-aspartate-alpha-decarboxylase; ADC; panD gene; drug target;

D O I：

10.1002/prot.21126

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

L-aspartate-alpha-decarboxylase (ADC) is a critical regulatory enzyme in the pantothenate biosynthetic pathway and belongs to a small class of self-cleaving and pyruvoyl-dependent amino acid decarboxylases. The expression level of ADC in Mycobacterium tuberculosis (Mtb) was confirmed by cDNA analysis, immunoblotting with an anti-ADC polyclonal antibody using whole cell lysate and immuno-electron microscopy. The recombinant ADC proenzyme from Mycobacterium tuberculosis (MtbADC) was overexpressed in E. coli and the protein structure was determined at 2.99 A resolution. The proteins fold into the double-psi beta-barrel structure. The subunits of the two tetramers (there are eight ADC molecules in the asymmetric unit) form pseudo fourfold rotational symmetry, similar to the E. coli ADC proenzyme structure. As pantothenate is synthesized in microorganisms, plants, and fungi but not in animals, structure elucidation of Mtb ADC is of substantial interest for structure-based drug development.

引用

页码：796 / 802

页数：7

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