4omt
Crystal structure of human muscle phosphofructokinase (dissociated homodimer)Crystal structure of human muscle phosphofructokinase (dissociated homodimer)
Structural highlights
DiseasePFKAM_HUMAN Glycogen storage disease due to muscle phosphofructokinase deficiency. The disease is caused by variants affecting the gene represented in this entry. FunctionPFKAM_HUMAN Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. Publication Abstract from PubMedWhereas 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 A resolution. The 3.2 A 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. Crystallization and preliminary crystallographic analysis of human muscle phosphofructokinase, the main regulator of glycolysis.,Kloos M, Bruser A, Kirchberger J, Schoneberg T, Strater N Acta Crystallogr F Struct Biol Commun. 2014 May;70(Pt 5):578-82. doi:, 10.1107/S2053230X14008723. Epub 2014 Apr 25. PMID:24817713[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||