Crystal structure of gluconate 5-dehydrogenase from Lentibacter algarum

Acta Crystallogr F Struct Biol Commun. 2020 May 1;76(Pt 5):228-234. doi: 10.1107/S2053230X20005336. Epub 2020 Apr 29.

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.

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

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / metabolism
  • Models, Molecular
  • Oxidoreductases / chemistry*
  • Oxidoreductases / genetics
  • Phylogeny
  • Protein Conformation, alpha-Helical
  • Protein Conformation, beta-Strand
  • Protein Multimerization
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Rhodobacteraceae / chemistry*
  • Rhodobacteraceae / enzymology
  • Sequence Alignment

Substances

  • Bacterial Proteins
  • Recombinant Proteins
  • Oxidoreductases
  • gluconate 5-dehydrogenase

Supplementary concepts

  • Lentibacter algarum