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Structures of citrate synthase and malate dehydrogenase of M ycobacterium tuberculosis
Author(s) -
Ferraris Davide M.,
Spallek Ralf,
Oehlmann Wulf,
Singh Mahavir,
Rizzi Menico
Publication year - 2015
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.24743
Subject(s) - citric acid cycle , malate dehydrogenase , citrate synthase , mycobacterium tuberculosis , biochemistry , malate synthase , enzyme , bacteria , dehydrogenase , metabolism , tricarboxylic acid , atp synthase , biology , tuberculosis , chemistry , microbiology and biotechnology , glyoxylate cycle , isocitrate lyase , medicine , genetics , pathology
The tricarboxylic acid (TCA) cycle is a central metabolic pathway of all aerobic organisms and is responsible for the synthesis of many important precursors and molecules. TCA cycle plays a key role in the metabolism of Mycobacterium tuberculosis and is involved in the adaptation process of the bacteria to the host immune response. We present here the first crystal structures of M. tuberculosis malate dehydrogenase and citrate synthase, two consecutive enzymes of the TCA, at 2.6 Å and 1.5 Å resolution, respectively. General analogies and local differences with the previously reported homologous protein structures are described. Proteins 2015; 83:389–394. © 2014 Wiley Periodicals, Inc.