Structure of Toxoplasma gondii fructose-1,6-bisphosphate aldolase

Lauren E. Boucher, Jürgen Bosch

Research output: Contribution to journalArticlepeer-review

Abstract

The apicomplexan parasite Toxoplasma gondii must invade host cells to continue its lifecycle. It invades different cell types using an actomyosin motor that is connected to extracellular adhesins via the bridging protein fructose-1,6-bisphosphate aldolase. During invasion, aldolase serves in the role of a structural bridging protein, as opposed to its normal enzymatic role in the glycolysis pathway. Crystal structures of the homologous Plasmodium falciparum fructose-1,6-bisphosphate aldolase have been described previously. Here, T. gondii fructose-1,6-bisphosphate aldolase has been crystallized in space group P22121, with the biologically relevant tetramer in the asymmetric unit, and the structure has been determined via molecular replacement to a resolution of 2.0Å. An analysis of the quality of the model and of the differences between the four chains in the asymmetric unit and a comparison between the T. gondii and P. falciparum aldolase structures is presented.

Original languageEnglish (US)
Pages (from-to)1186-1192
Number of pages7
JournalActa Crystallographica Section:F Structural Biology Communications
Volume70
DOIs
StatePublished - Sep 1 2014

Keywords

  • aldolase
  • F16BP
  • glideosome
  • invasion
  • MIC2
  • Toxoplasma

ASJC Scopus subject areas

  • Biophysics
  • Genetics
  • Structural Biology
  • Condensed Matter Physics
  • Biochemistry

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