2HIG
Crystal Structure of Phosphofructokinase apoenzyme from Trypanosoma brucei.
Summary for 2HIG
| Entry DOI | 10.2210/pdb2hig/pdb |
| Descriptor | 6-phospho-1-fructokinase, SODIUM ION (3 entities in total) |
| Functional Keywords | transferase |
| Biological source | Trypanosoma brucei |
| Total number of polymer chains | 2 |
| Total formula weight | 107232.68 |
| Authors | Martinez-Oyanedel, J.,McNae, I.W.,Fothergill-Gilmore, L.A.,Walkinshaw, M.D. (deposition date: 2006-06-29, release date: 2007-02-13, Last modification date: 2024-02-14) |
| Primary citation | Martinez-Oyanedel, J.,McNae, I.W.,Nowicki, M.W.,Keillor, J.W.,Michels, P.A.,Fothergill-Gilmore, L.A.,Walkinshaw, M.D. The First Crystal Structure of Phosphofructokinase from a Eukaryote: Trypanosoma brucei. J.Mol.Biol., 366:1185-1198, 2007 Cited by PubMed Abstract: The crystal structure of the ATP-dependent phosphofructokinase (PFK) from Trypanosoma brucei provides the first detailed description of a eukaryotic PFK, and enables comparisons to be made with the crystal structures of bacterial ATP-dependent and PPi-dependent PFKs. The structure reveals that two insertions (the 17-20 and 329-348 loops) that are characteristic of trypanosomatid PFKs, but absent from bacterial and mammalian ATP-dependent PFKs, are located within and adjacent to the active site, and are in positions to play important roles in the enzyme's mechanism. The 90 residue N-terminal extension forms a novel domain that includes an "embracing arm" across the subunit boundary to the symmetry-related subunit in the tetrameric enzyme. Comparisons with the PPi-dependent PFK from Borrelia burgdorferi show that several features thought to be characteristic of PPi-dependent PFKs are present in the trypanosome ATP-dependent PFK. These two enzymes are generally more similar to each other than to the bacterial or mammalian ATP-dependent PFKs. However, there are critical differences at the active site of PPi-dependent PFKs that are sufficient to prevent the binding of ATP. This crystal structure of a eukaryotic PFK has enabled us to propose a detailed model of human muscle PFK that shows active site and other differences that offer opportunities for structure-based drug discovery for the treatment of sleeping sickness and other diseases caused by the trypanosomatid family of protozoan parasites. PubMed: 17207816DOI: 10.1016/j.jmb.2006.10.019 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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