4TVM

Structure of Citrate Synthase from Mycobacterium tuberculosis

Summary for 4TVM

Entry DOI	10.2210/pdb4tvm/pdb
Descriptor	Citrate synthase, OXALOACETATE ION (3 entities in total)
Functional Keywords	krebs cycle, transferase
Biological source	Mycobacterium tuberculosis
Total number of polymer chains	1
Total formula weight	48132.28
Authors	Ferraris, D.M.,Rizzi, M. (deposition date: 2014-06-27, release date: 2015-01-14, Last modification date: 2023-12-20)
Primary citation	Ferraris, D.M.,Spallek, R.,Oehlmann, W.,Singh, M.,Rizzi, M. Structures of citrate synthase and malate dehydrogenase of Mycobacterium tuberculosis. Proteins, 83:389-394, 2015 Cited by PubMed Abstract: 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. PubMed: 25524525 DOI: 10.1002/prot.24743 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.6 Å)

Structure validation