Crystal structure of a reconstructed ancestor of Triosephosphate isomerase from eukaryotes

Structural, thermodynamic and catalytic characterization of an ancestral triosephosphate isomerase reveal early evolutionary coupling between monomer association and function.

MASRKFFVGGNWKMNGTLESIKALVETLNSAQLDPNTEVVVAPPAIYLPFARSKLKKPKEIQVAAQNCYTKPNGAFTGEI
SAEMLKDLGVPWVILGHSERRTIFGESDELIAEKVKYALDQGLKVIACIGETLEEREAGKTMEVVARQILKAIADKIKDW
SNVVIAYEPVWAIGTGKVATPEQAQEVHAALRKWLKENVSPEVAESTRIIYGGSVNAANCKELAKQPDIDGFLVGGASLK
APEFVDIINARQ

0.1M HEPS pH 7.5, 20% PEG 8000.
Protein concentration 6 mg/mL in 10 mM Triethanolamine pH 7.6, 1 mM EDTA, 1 mM DTT, 50 mM NaCl, 10 mM PGH

Isomerase, Glycolisis, TIM Barrel, Ancestral sequence reconstruction