Crystal structure of gluconate 5-dehydrogenase from Lentibacter algarum

摘要

Gluconate 5-dehydrogenase (Ga5DH; EC 1.1.1.69) from Lentibacter algarum (LaGa5DH) was recombinantly expressed in Escherichia coli and purified to homogeneity. The protein was crystallized and the crystal structure was solved at 2.1 angstrom resolution. The crystal belonged to the monoclinic system, with space group P1 and unit-cell parameters a = 55.42, b = 55.48, c = 79.16 angstrom, alpha = 100.51, beta = 105.66, gamma = 97.99 degrees. The structure revealed LaGaDH to be a tetramer, with each subunit consisting of six alpha-helices and three antiparallel beta-hairpins. LaGa5DH has high structural similarity to other Ga5DH proteins, demonstrating that this enzyme is highly conserved.

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