4OMT

Crystal structure of human muscle phosphofructokinase (dissociated homodimer)

4OMT の概要

• エントリーDOI: 10.2210/pdb4omt/pdb
• 関連するPDBエントリー: 3O8N 3OPY
• 分子名称: 6-phosphofructokinase, muscle type (1 entity in total)
• 機能のキーワード: human 6-phosphofructokinase, 6-phosphofructokinase activity, fructose 6-phosphate, transferase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 85294.52

構造登録者

Kloos, M.,Straeter, N. (登録日: 2014-01-27, 公開日: 2014-05-14, 最終更新日: 2023-09-20)

主引用文献

Kloos, M.,Bruser, A.,Kirchberger, J.,Schoneberg, T.,Strater, N.
Crystallization and preliminary crystallographic analysis of human muscle phosphofructokinase, the main regulator of glycolysis.
Acta Crystallogr F Struct Biol Commun, 70:578-582, 2014

PubMed Abstract: Whereas the three-dimensional structure and the structural basis of the allosteric regulation of prokaryotic 6-phosphofructokinases (Pfks) have been studied in great detail, knowledge of the molecular basis of the allosteric behaviour of the far more complex mammalian Pfks is still very limited. The human muscle isozyme was expressed heterologously in yeast cells and purified using a five-step purification protocol. Protein crystals suitable for diffraction experiments were obtained by the vapour-diffusion method. The crystals belonged to space group P6222 and diffracted to 6.0 Å resolution. The 3.2 Å resolution structure of rabbit muscle Pfk (rmPfk) was placed into the asymmetric unit and optimized by rigid-body and group B-factor refinement. Interestingly, the tetrameric enzyme dissociated into a dimer, similar to the situation observed in the structure of rmPfk.

PubMed: 24817713
DOI: 10.1107/S2053230X14008723

実験手法

X-RAY DIFFRACTION (6 Å)