Sandbox GGC7

Triosephosphate isomerase (TPI or TIM) is a functionally and structurally well-known enzyme that play a crucial role in glycolytic and gluconeogenic metabolism. TPI interconverts dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (G3P) ^[1]

Structure and Function

This crystal structure of trioseohosphate isomerase was isolated from Thermoplasma acidophilum, an archaeal species, and therefore was called TaTPI. TaTPI contain four copies of TaTPI monomer in the asymmetric unit, comprising two homodimers. TaTPI is composed of 216 amino acid residues, which is shorter compare to other TPIs from bacterial and eukaryotic species. Each subunit of homotetramer forms a TIM barrel in which 8α helices alternate with 8β sheets to form backbone of the protein. Hydrophobic chains form the core enzyme whereas hydrophilic found near the ends of the barrel where exposed to solvent. Each subunit has it own active site and only active as a dimer. The active site includes His 89, Glu137, Lys 9.

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Structural highlights

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