4TU1

Structure of Toxoplasma gondii fructose 1,6 bisphosphate aldolase

Summary for 4TU1

• Entry DOI: 10.2210/pdb4tu1/pdb
• Descriptor: Fructose-1,6-bisphosphate aldolase, GLYCEROL (3 entities in total)
• Functional Keywords: aldolase, f16bp, invasion, toxoplasma, glideosome, structural genomics, psi-2, protein structure initiative, seattle structural genomics center for infectious disease, ssgcid, lyase
• Biological source: Toxoplasma gondii
• Total number of polymer chains: 4
• Total formula weight: 154308.56

Authors

Boucher, L.E.,Bosch, J.,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2014-06-23, release date: 2014-09-03, Last modification date: 2023-09-27)

Primary citation

Boucher, L.E.,Bosch, J.
Structure of Toxoplasma gondii fructose-1,6-bisphosphate aldolase.
Acta Crystallogr.,Sect.F, 70:1186-1192, 2014

PubMed 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 2.0 Å. 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.

PubMed: 25195889
DOI: 10.1107/S2053230X14017087

Experimental method

X-RAY DIFFRACTION (2 Å)