2O2D
Crystal structure of phosphoglucose isomerase from Trypanosoma brucei complexed with citrate
Summary for 2O2D
Entry DOI | 10.2210/pdb2o2d/pdb |
Related | 2O2D |
Descriptor | Glucose-6-phosphate isomerase, glycosomal, CITRIC ACID, GLYCEROL, ... (4 entities in total) |
Functional Keywords | dimer, isomerase |
Biological source | Trypanosoma brucei brucei |
Cellular location | Glycosome: P13377 |
Total number of polymer chains | 3 |
Total formula weight | 206228.62 |
Authors | Arsenieva, D.,Mazock, G.H.,Appavu, B.L.,Jeffery, C.J. (deposition date: 2006-11-29, release date: 2007-11-13, Last modification date: 2023-08-30) |
Primary citation | Arsenieva, D.,Appavu, B.L.,Mazock, G.H.,Jeffery, C.J. Crystal structure of phosphoglucose isomerase from Trypanosoma brucei complexed with glucose-6-phosphate at 1.6 A resolution Proteins, 74:72-80, 2008 Cited by PubMed Abstract: Enzymes of glycolysis in Trypanosoma brucei have been identified as potential drug targets for African sleeping sickness because glycolysis is the only source of ATP for the bloodstream form of this parasite. Several inhibitors were previously reported to bind preferentially to trypanosomal phosphoglucose isomerase (PGI, the second enzyme in glycolysis) than to mammalian PGIs, which suggests that PGI might make a good target for species-specific drug design. Herein, we report recombinant expression, purification, crystallization and X-ray crystal structure determination of T. brucei PGI. One structure solved at 1.6 A resolution contains a substrate, D-glucose-6-phosphate, in an extended conformation in the active site. A second structure solved at 1.9 A resolution contains a citrate molecule in the active site. The structures are compared with the crystal structures of PGI from humans and from Leishmania mexicana. The availability of recombinant tPGI and its first high-resolution crystal structures are initial steps in considering this enzyme as a potential drug target. PubMed: 18561188DOI: 10.1002/prot.22133 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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