6TEP
Crystal structure of a galactokinase from Bifidobacterium infantis in complex with ADP
Summary for 6TEP
Entry DOI | 10.2210/pdb6tep/pdb |
Descriptor | Galactokinase, DI(HYDROXYETHYL)ETHER, GLYCEROL, ... (8 entities in total) |
Functional Keywords | adp, complex, galactokinase, transferase |
Biological source | Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12) |
Total number of polymer chains | 4 |
Total formula weight | 187435.18 |
Authors | Keenan, T.,Parmeggiani, F.,Fontenelle, C.Q.,Malassis, J.,Vendeville, J.,Offen, W.A.,Both, P.,Huang, K.,Marchesi, A.,Heyam, A.,Young, C.,Charnock, S.,Davies, G.J.,Linclau, B.,Flitsch, S.L.,Fascione, M.A. (deposition date: 2019-11-12, release date: 2020-06-10, Last modification date: 2024-01-24) |
Primary citation | Keenan, T.,Parmeggiani, F.,Malassis, J.,Fontenelle, C.Q.,Vendeville, J.B.,Offen, W.,Both, P.,Huang, K.,Marchesi, A.,Heyam, A.,Young, C.,Charnock, S.J.,Davies, G.J.,Linclau, B.,Flitsch, S.L.,Fascione, M.A. Profiling Substrate Promiscuity of Wild-Type Sugar Kinases for Multi-fluorinated Monosaccharides. Cell Chem Biol, 27:1199-, 2020 Cited by PubMed Abstract: Fluorinated sugar-1-phosphates are of emerging importance as intermediates in the chemical and biocatalytic synthesis of modified oligosaccharides, as well as probes for chemical biology. Here we present a systematic study of the activity of a wide range of anomeric sugar kinases (galacto- and N-acetylhexosamine kinases) against a panel of fluorinated monosaccharides, leading to the first examples of polyfluorinated substrates accepted by this class of enzymes. We have discovered four new N-acetylhexosamine kinases with a different substrate scope, thus expanding the number of homologs available in this subclass of kinases. Lastly, we have solved the crystal structure of a galactokinase in complex with 2-deoxy-2-fluorogalactose, giving insight into changes in the active site that may account for the specificity of the enzyme toward certain substrate analogs. PubMed: 32619452DOI: 10.1016/j.chembiol.2020.06.005 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
Download full validation report
