6B6U

Pyruvate Kinase M2 mutant - S437Y

6B6U の概要

• エントリーDOI: 10.2210/pdb6b6u/pdb
• 分子名称: Pyruvate kinase PKM, 1,2-ETHANEDIOL, MAGNESIUM ION, ... (11 entities in total)
• 機能のキーワード: glycolysis, gene regulation, phosphotransferase, transferase
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm : P14618
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 116495.61

構造登録者

Srivastava, D.,Dey, M. (登録日: 2017-10-03, 公開日: 2017-12-20, 最終更新日: 2023-10-04)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.35 Å)