3h4t | pdb_00003h4t
Chimeric Glycosyltransferase for the generation of novel natural products - GtfAH1 in complex with UDP-2F-Glc
Structural highlights
FunctionGTFA_AMYOR Catalyzes the attachment of 4-epi-vancosamine from a TDP donor to the beta-OH-Tyr-6 of the aglycone cosubstrate in the biosynthesis of glycopeptide antibiotic chloroeremomycin, a member of the vancomycin group of antibiotics. Strongly prefers devancoaminyl-vancomycin (DVV) as substrate rather than the heptapeptide vancomycin aglycone (AGV). Acts downstream of GtfB.[1] [2] [3] Q6ZZJ7_ACTTI Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedGlycodiversification, 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. Chimeric glycosyltransferases for the generation of hybrid glycopeptides.,Truman AW, Dias MV, Wu S, Blundell TL, Huang F, Spencer JB Chem Biol. 2009 Jun 26;16(6):676-85. PMID:19549605[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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