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6TEP

Crystal structure of a galactokinase from Bifidobacterium infantis in complex with ADP

Summary for 6TEP
Entry DOI10.2210/pdb6tep/pdb
DescriptorGalactokinase, DI(HYDROXYETHYL)ETHER, GLYCEROL, ... (8 entities in total)
Functional Keywordsadp, complex, galactokinase, transferase
Biological sourceBifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12)
Total number of polymer chains4
Total formula weight187435.18
Authors
Primary citationKeenan, 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: 32619452
DOI: 10.1016/j.chembiol.2020.06.005
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.45 Å)
Structure validation

237735

数据于2025-06-18公开中

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