Structures of citrate synthase and malate dehydrogenase of Mycobacterium tuberculosis

Proteins. 2015 Feb;83(2):389-94. doi: 10.1002/prot.24743. Epub 2015 Jan 7.

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.

Keywords: Krebs cycle; Mycobacterium tuberculosis; tricarboxylic acid cycle; tuberculosis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Catalytic Domain
  • Citrate (si)-Synthase / chemistry*
  • Conserved Sequence
  • Crystallography, X-Ray
  • Malate Dehydrogenase / chemistry*
  • Models, Molecular
  • Molecular Sequence Data
  • Mycobacterium tuberculosis / enzymology
  • Protein Structure, Secondary

Substances

  • Bacterial Proteins
  • Malate Dehydrogenase
  • Citrate (si)-Synthase

Associated data

  • PDB/4TVM
  • PDB/4TVO