Molecular Dynamics Study of Triazole Derivative Binding to the Active Site of Imidazole Glycerol Phosphate Dehydratase from Mycobacterium tuberculosis

Agapova, Yu. K.; Тимофеев, В. И.; Комолов, А. С.

doi:10.1134/s1063774519040023

Cited by 3 publications

(1 citation statement)

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“…Other bacterial genomes harbor bifunctional genes, in which IGPD coding gene is fused to the histidinol-phosphate phosphatase one, the penultimate enzyme of histidine biosynthesis [17]. Previous structures of IGPDs available in the PDB, belonging to all the three cell lineages, show that IGPD is a homo 24-mer with, correspondingly, 24 active sites, each formed by residues from three adjacent subunits [53], and that it presents two manganese ions bound at each of the catalytic centers [52]. This structure and other biochemical data reveal that, unlike other enzymes in which Mn 2+ can be exchanged with Mg 2+ or Zn 2+ with little effect on activity, IGPD has a peculiar requirement for manganese [47]; indeed, in the absence of Mn 2+ , plant and fungal IGPDs are stable but inactive trimers [52].…”

Section: Hisbmentioning

confidence: 99%

The Role of Gene Elongation in the Evolution of Histidine Biosynthetic Genes

et al. 2020

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Gene elongation is a molecular mechanism consisting of an in-tandem duplication of a gene and divergence and fusion of the two copies, resulting in a gene constituted by two divergent paralogous modules. The aim of this work was to evaluate the importance of gene elongation in the evolution of histidine biosynthetic genes and to propose a possible evolutionary model for some of them. Concerning the genes hisA and hisF, which code for two homologous (β/α)8-barrels, it has been proposed that the two extant genes could be the result of a cascade of gene elongation/domain shuffling events starting from an ancestor gene coding for just one (β/α) module. A gene elongation event has also been proposed for the evolution of hisB and hisD; structural analyses revealed the possibility of an early elongation event, resulting in the repetition of modules. Furthermore, it is quite possible that the gene elongations responsible for the evolution of the four proteins occurred before the earliest phylogenetic divergence. In conclusion, gene elongation events seem to have played a crucial role in the evolution of the histidine biosynthetic pathway, and they may have shaped the structures of many genes during the first steps of their evolution.

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