Crystallization and preliminary crystallographic analysis of human muscle phosphofructokinase, the main regulator of glycolysis. Issue 5 (1st May 2014)

• Record Type: Journal Article
• Authors: Kloos, Marco; Brüser, Antje; Kirchberger, Jürgen; Schöneberg, Torsten; Sträter, Norbert
• Is Part Of: Acta crystallographica. Volume 70:Issue 5(2014:May)
• Page Start: 578
• Page End: 582
• Publication Date: 2014-05-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X14008723
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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 <italic>P</italic>6₂22 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 <italic>B</italic>‐factor refinement. Interestingly, the tetrameric enzyme dissociated into a dimer, similar to the situation observed in the structure of rmPfk.</p> </abstract>