3OTR

2.75 Angstrom Crystal Structure of Enolase 1 from Toxoplasma gondii

Summary for 3OTR

• Entry DOI: 10.2210/pdb3otr/pdb
• Descriptor: Enolase, CHLORIDE ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: structural genomics, center for structural genomics of infectious diseases, csgid, alpha-beta barrel, tim barrel, enolase 1 like n-terminal domain, 2-phospho-d-glycerate hydrolase, lyase
• Biological source: Toxoplasma gondii
• Total number of polymer chains: 6
• Total formula weight: 296996.28

Authors

Minasov, G.,Ruan, J.,Shuvalova, L.,Halavaty, A.,Ngo, H.,Tomavo, S.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2010-09-13, release date: 2010-09-22, Last modification date: 2023-09-06)

Primary citation

Ruan, J.,Mouveaux, T.,Light, S.H.,Minasov, G.,Anderson, W.F.,Tomavo, S.,Ngo, H.M.
The structure of bradyzoite-specific enolase from Toxoplasma gondii reveals insights into its dual cytoplasmic and nuclear functions.
Acta Crystallogr.,Sect.D, 71:417-426, 2015

PubMed Abstract: In addition to catalyzing a central step in glycolysis, enolase assumes a remarkably diverse set of secondary functions in different organisms, including transcription regulation as documented for the oncogene c-Myc promoter-binding protein 1. The apicomplexan parasite Toxoplasma gondii differentially expresses two nuclear-localized, plant-like enolases: enolase 1 (TgENO1) in the latent bradyzoite cyst stage and enolase 2 (TgENO2) in the rapidly replicative tachyzoite stage. A 2.75 Å resolution crystal structure of bradyzoite enolase 1, the second structure to be reported of a bradyzoite-specific protein in Toxoplasma, captures an open conformational state and reveals that distinctive plant-like insertions are located on surface loops. The enolase 1 structure reveals that a unique residue, Glu164, in catalytic loop 2 may account for the lower activity of this cyst-stage isozyme. Recombinant TgENO1 specifically binds to a TTTTCT DNA motif present in the cyst matrix antigen 1 (TgMAG1) gene promoter as demonstrated by gel retardation. Furthermore, direct physical interactions of both nuclear TgENO1 and TgENO2 with the TgMAG1 gene promoter are demonstrated in vivo using chromatin immunoprecipitation (ChIP) assays. Structural and biochemical studies reveal that T. gondii enolase functions are multifaceted, including the coordination of gene regulation in parasitic stage development. Enolase 1 provides a potential lead in the design of drugs against Toxoplasma brain cysts.

PubMed: 25760592
DOI: 10.1107/S1399004714026479

Experimental method

X-RAY DIFFRACTION (2.75 Å)