5AQ1
Trypanosoma cruzi Glucose-6-phosphate Dehydrogenase in complex with G6P and NADPH
Summary for 5AQ1
| Entry DOI | 10.2210/pdb5aq1/pdb |
| Descriptor | GLUCOSE-6-PHOSPHATE DEHYDROGENASE, 6-O-phosphono-beta-D-glucopyranose, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total) |
| Functional Keywords | oxidoreductase, pentose phosphate pathway, redox balance, chagas disease, g6pd, g6pdh. |
| Biological source | TRYPANOSOMA CRUZI |
| Total number of polymer chains | 3 |
| Total formula weight | 175878.02 |
| Authors | Mercaldi, G.F.,Dawson, A.,Hunter, W.N.,Cordeiro, A.T. (deposition date: 2015-09-18, release date: 2016-07-20, Last modification date: 2024-11-06) |
| Primary citation | Mercaldi, G.F.,Dawson, A.,Hunter, W.N.,Cordeiro, A.T. The Structure of a Trypanosoma Cruzi Glucose-6-Phosphate Dehydrogenase Reveals Differences from the Mammalian Enzyme. FEBS Lett., 590:2776-, 2016 Cited by PubMed Abstract: The enzyme glucose-6-phosphate dehydrogenase from Trypanosoma cruzi (TcG6PDH) catalyses the first step of the pentose phosphate pathway (PPP) and is considered a promising target for the discovery of a new drug against Chagas diseases. In the present work, we describe the crystal structure of TcG6PDH obtained in a ternary complex with the substrate β-d-glucose-6-phosphate (G6P) and the reduced 'catalytic' cofactor NADPH, which reveals the molecular basis of substrate and cofactor recognition. A comparison with the homologous human protein sheds light on differences in the cofactor-binding site that might be explored towards the design of new NADP(+) competitive inhibitors targeting the parasite enzyme. PubMed: 27391210DOI: 10.1002/1873-3468.12276 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.65 Å) |
Structure validation
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