6LE3
Crystal structure of gluconate 5-dehydrogenase from Lentibacter algarum
Summary for 6LE3
Entry DOI | 10.2210/pdb6le3/pdb |
Descriptor | Gluconate 5-dehydrogenase, ACETYL GROUP (3 entities in total) |
Functional Keywords | gluconate 5-dehydrogenase, biosynthetic protein |
Biological source | Lentibacter algarum |
Total number of polymer chains | 4 |
Total formula weight | 108894.86 |
Authors | Yuan, H. (deposition date: 2019-11-23, release date: 2020-05-13, Last modification date: 2023-11-22) |
Primary citation | Tian, D.,Fu, X.,Cao, W.,Yuan, H. Crystal structure of gluconate 5-dehydrogenase from Lentibacter algarum. Acta Crystallogr.,Sect.F, 76:228-234, 2020 Cited by PubMed 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. PubMed: 32356525DOI: 10.1107/S2053230X20005336 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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