Structural highlights
Function
A0A1H3NGY9_9RHOB
Publication Abstract from PubMed
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 A 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 A, 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.
Crystal structure of gluconate 5-dehydrogenase from Lentibacter algarum.,Tian D, Fu X, Cao W, Yuan H Acta Crystallogr F Struct Biol Commun. 2020 May 1;76(Pt 5):228-234. doi:, 10.1107/S2053230X20005336. Epub 2020 Apr 29. PMID:32356525[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tian D, Fu X, Cao W, Yuan H. Crystal structure of gluconate 5-dehydrogenase from Lentibacter algarum. Acta Crystallogr F Struct Biol Commun. 2020 May 1;76(Pt 5):228-234. PMID:32356525 doi:10.1107/S2053230X20005336
