7JH0
Crystallographic structure of glyceraldehyde-3-phosphate dehydrogenase from Schistosoma mansoni
Summary for 7JH0
Entry DOI | 10.2210/pdb7jh0/pdb |
Descriptor | Glyceraldehyde-3-phosphate dehydrogenase, GLYCEROL, TRIETHYLENE GLYCOL, ... (7 entities in total) |
Functional Keywords | oxidoreductase |
Biological source | Schistosoma mansoni (Blood fluke) More |
Total number of polymer chains | 4 |
Total formula weight | 146725.17 |
Authors | Boreiko, S.,Silva, M.,Iulek, J. (deposition date: 2020-07-20, release date: 2021-02-17, Last modification date: 2023-10-18) |
Primary citation | Boreiko, S.,Silva, M.,Iulek, J. Structure determination and analyses of the GAPDH from the parasite Schistosoma mansoni, the first one from a platyhelminth. Biochimie, 184:18-25, 2021 Cited by PubMed Abstract: The enzyme Glyceraldehyde-3-Phosphate Dehydrogenase from Schistosoma mansoni (SmGAPDH) is characterized as a therapeutical target for schistosomiasis. In this context, we report here the experimental structure, structural analyses and comparisons of SmGAPDH, the first one from a Platyhelminth. The enzyme was expressed, purified and assayed for crystallization, what allowed the obtainment of crystals of sufficient quality to collect X-ray diffraction data up to 2.51 Å resolution. SmGAPDH is the only GAPDH to present the sequence NNR (its residues 114-116) which leads to (especially R116) a hydrogen bond network that possibly reflects on the flexibility of residues to interact with the adenine part of NAD, speculated to be important for differential drug design. PubMed: 33524435DOI: 10.1016/j.biochi.2021.01.014 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.51 Å) |
Structure validation
Download full validation report