2hig | pdb_00002hig

Crystal Structure of Phosphofructokinase apoenzyme from Trypanosoma brucei.

spinqualitylabelsall models 2hig, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2hig is a 2 chain structure with sequence from Trypanosoma (trypanozoon) brucei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NA Gene: pfk (Trypanosoma (Trypanozoon) brucei) Activity: 6-phosphofructokinase, with EC number 2.7.1.11 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [PFKA_TRYBB] Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.[HAMAP-Rule:MF_03186] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. The first crystal structure of phosphofructokinase from a eukaryote: Trypanosoma brucei.,Martinez-Oyanedel J, McNae IW, Nowicki MW, Keillor JW, Michels PA, Fothergill-Gilmore LA, Walkinshaw MD J Mol Biol. 2007 Mar 2;366(4):1185-98. Epub 2006 Oct 11. PMID:17207816 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphofructokinase (PFK)

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