3H4T

Chimeric Glycosyltransferase for the generation of novel natural products - GtfAH1 in complex with UDP-2F-Glc

Summary for 3H4T

• Entry DOI: 10.2210/pdb3h4t/pdb
• Related: 3H4I
• Descriptor: Glycosyltransferase GtfA, Glycosyltransferase, PHOSPHATE ION, URIDINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: glycosyltransferase, vancomycin, teicoplanin, gtfa, orf1, natural products, antibiotic, transferase
• Biological source: Amycolatopsis orientalis; More
• Total number of polymer chains: 1
• Total formula weight: 42891.63

Authors

Dias, M.V.B.,Truman, A.W.,Wu, S.,Blundell, T.L.,Huang, F.,Spencer, J.B. (deposition date: 2009-04-20, release date: 2009-07-28, Last modification date: 2023-11-01)

Primary citation

Truman, A.W.,Dias, M.V.B.,Wu, S.,Blundell, T.L.,Huang, F.,Spencer, J.B.
Chimeric glycosyltransferases for the generation of hybrid glycopeptides
Chem.Biol., 16:676-685, 2009

PubMed Abstract: Glycodiversification, an invaluable tool for generating biochemical diversity, can be catalyzed by glycosyltransferases, which attach activated sugar "donors" onto "acceptor" molecules. However, many glycosyltransferases can tolerate only minor modifications to their native substrates, thus making them unsuitable tools for current glycodiversification strategies. Here we report the production of functional chimeric glycosyltransferases by mixing and matching the N- and C-terminal domains of glycopeptide glycosyltransferases. Using this method we have generated hybrid glycopeptides and have demonstrated that domain swapping can result in a predictable switch of substrate specificity, illustrating that N- and C-terminal domains predominantly dictate acceptor and donor specificity, respectively. The determination of the structure of a chimera in complex with a sugar donor analog shows that almost all sugar-glycosyltransferase binding interactions occur in the C-terminal domain.

PubMed: 19549605
DOI: 10.1016/j.chembiol.2009.04.013

Experimental method

X-RAY DIFFRACTION (1.15 Å)