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Crystal structure of uncleaved L ‐aspartate‐α‐decarboxylase from Mycobacterium tuberculosis
Author(s) -
Gopalan Gayathri,
Chopra Sidharth,
Ranganathan Anand,
Swaminathan Kunchithapadam
Publication year - 2006
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.21126
Subject(s) - mycobacterium tuberculosis , recombinant dna , polyclonal antibodies , complementary dna , biochemistry , microbiology and biotechnology , chemistry , immunoelectron microscopy , glutamate decarboxylase , mycobacterium , enzyme , biology , stereochemistry , bacteria , antibody , tuberculosis , gene , medicine , genetics , pathology , immunology
L ‐aspartate‐α‐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 immunoelectron microscopy. The recombinant ADC proenzyme from Mycobacterium tuberculosis (MtbADC) was overexpressed in E. coli and the protein structure was determined at 2.99 Å resolution. The proteins fold into the double‐ψ β‐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. Proteins 2006. © 2006 Wiley‐Liss, Inc.