Pyruvate Decarboxylase - Structure

Structure

Pyruvate decarboxylase occurs as a dimer of dimers with two active sites shared between the monomers of each dimer. The enzyme contains a beta-alpha-beta structure, yielding parallel beta-sheets. It contains 563 residue subunits in each dimer; the enzyme has strong intermonomer attractions, but the dimers loosely interact to form a loose tetramer.

Crystallographic structures of pyruvate decarboxylase
Cartoon diagram of pyruvate decarboxylase monomer with TPP attached.
Cartoon diagram of pyruvate decarboxylase tetramer.
Active site of pyruvate decarboxylase with selected amino acids: Glu-51, Glu-477, Asp-444, and Asp-28. Also displayed are cofactors TPP and Mg2+.
Positions of His and Cys residues in respect to active site (TPP and Mg) that participate in conformation changes when interacting with pyruvate substrate.

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