2HIG

Crystal Structure of Phosphofructokinase apoenzyme from Trypanosoma brucei.

2HIG の概要

• エントリーDOI: 10.2210/pdb2hig/pdb
• 分子名称: 6-phospho-1-fructokinase, SODIUM ION (3 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: Trypanosoma brucei
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 107232.68

構造登録者

Martinez-Oyanedel, J.,McNae, I.W.,Fothergill-Gilmore, L.A.,Walkinshaw, M.D. (登録日: 2006-06-29, 公開日: 2007-02-13, 最終更新日: 2024-02-14)

主引用文献

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

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: 17207816
DOI: 10.1016/j.jmb.2006.10.019

実験手法

X-RAY DIFFRACTION (2.4 Å)