6B6U

Pyruvate Kinase M2 mutant - S437Y

Summary for 6B6U

• Entry DOI: 10.2210/pdb6b6u/pdb
• Descriptor: Pyruvate kinase PKM, 1,2-ETHANEDIOL, MAGNESIUM ION, ... (11 entities in total)
• Functional Keywords: glycolysis, gene regulation, phosphotransferase, transferase
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm : P14618
• Total number of polymer chains: 2
• Total formula weight: 116495.61

Authors

Srivastava, D.,Dey, M. (deposition date: 2017-10-03, release date: 2017-12-20, Last modification date: 2023-10-04)

Primary citation

Srivastava, D.,Razzaghi, M.,Henzl, M.T.,Dey, M.
Structural Investigation of a Dimeric Variant of Pyruvate Kinase Muscle Isoform 2.
Biochemistry, 56:6517-6520, 2017

PubMed Abstract: Pyruvate kinase muscle isoform 2 (PKM2) catalyzes the terminal step in glycolysis, transferring a phosphoryl group from phosphoenolpyruvate to ADP, to produce pyruvate and ATP. PKM2 activity is allosterically regulated by fructose 1,6-bisphosphate (FBP), an upstream glycolytic intermediate. FBP stabilizes the tetrameric form of the enzyme. In its absence, the PKM2 tetramers dissociate, yielding a dimer-monomer mixture having lower enzymatic activity. The S437Y variant of PKM2 is incapable of binding FBP. Consistent with that defect, we find that S437Y exists in a monomer-dimer equilibrium in solution, with a K of ∼20 μM. Interestingly, however, the protein crystallizes as a tetramer, providing insight into the structural basis for impaired FBP binding of S437Y.

PubMed: 29182273
DOI: 10.1021/acs.biochem.7b01013

Experimental method

X-RAY DIFFRACTION (1.35 Å)