10GI

Structure of Glyceraldehyde-3-Phosphate Dehydrogenase from Babesia bovis

Summary for 10GI

• Entry DOI: 10.2210/pdb10gi/pdb
• Descriptor: Glyceraldehyde-3-phosphate dehydrogenase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• Functional Keywords: bovine babesiosis, babesia bovis, gapdh, structural genomics, seattle structural genomics center for infectious disease, ssgcid, oxidoreductase
• Biological source: Babesia bovis
• Total number of polymer chains: 2
• Total formula weight: 78334.42

Authors

Ukrainski, B.,Galvao, E.B.,Silva, M.,Iulek, J.,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2026-01-19, release date: 2026-08-19, Last modification date: 2026-08-26)

Primary citation

Ukrainski, B.,Galvao, E.B.,Silva, M.,Iulek, J.
Expression, purification, crystallization and structure solution of glyceraldehyde-3-phosphate dehydrogenase from the babesiosis infective agent Babesia bovis.
Protein Expr.Purif., 243:106991-106991, 2026

PubMed Abstract: Babesia bovis is a species of apicomplexan hemoparasitic protozoa that can be transmitted by ticks, causing a global cattle disease. As it depends mainly on the glycolytic pathway for energy production and life cycle maintenance, glycolytic enzymes are possible targets for drug development against Babesia. Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) has been one of such targets, against several parasitic organisms. It performs the reversible oxidative phosphorylation of glyceraldehyde-3-phosphate to 1,3-bisphospho-D-glycerate in the presence of nicotinamide adenine dinucleotide. The protocol for Babesia bovis Glyceraldehyde-3-Phosphate Dehydrogenase (BbGAPDH) expression and purification has been developed to yields of 28 mg of pure protein per liter of culture medium, with a specific activity of 55.5 ± 6.99 U mg after His-tag removal, indicating preservation of enzymatic activity. For crystallization, the His-tag removal proved essential. Crystals diffracted to 3.12 Å resolution in the P321 space group; NAD cofactor molecules are observed in their respective sites. Comparisons to the theoretical model indicate a number of side chain conformation differences. These results provide support for future enzyme inhibition assays, in addition to crystallization assays with potential inhibitors.

PubMed: 42600714
DOI: 10.1016/j.pep.2026.106991

Experimental method

X-RAY DIFFRACTION (3.12 Å)