Literature DB >> 32356525

Crystal structure of gluconate 5-dehydrogenase from Lentibacter algarum.

Dengke Tian1, Xueqi Fu1, Wenqiang Cao1, Hong Yuan2.   

Abstract

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 Å 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 Å, α = 100.51, β = 105.66, γ = 97.99°. The structure revealed LaGaDH to be a tetramer, with each subunit consisting of six α-helices and three antiparallel β-hairpins. LaGa5DH has high structural similarity to other Ga5DH proteins, demonstrating that this enzyme is highly conserved.

Entities:  

Keywords:  Lentibacter algarum; crystal structure; gluconate 5-dehydrogenase

Mesh：

Substances：

Year:  2020        PMID： 32356525      PMCID： PMC7193515          DOI： 10.1107/S2053230X20005336

Source DB:  PubMed          Journal:  Acta Crystallogr F Struct Biol Commun        ISSN： 2053-230X            Impact factor:   1.056


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