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Biochemistry. 2010 May 18;49(19):4159-68. doi: 10.1021/bi100150v.

Crystal structures of the glycopeptide sulfotransferase Teg12 in a complex with the teicoplanin aglycone.

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Howard Hughes Medical Institute, Laboratory of Genetically Encoded Small Molecules, Laboratory of Molecular Biophysics, The Rockefeller University, 1230 York Avenue, New York, New York 10065, USA.


The TEG gene cluster, a glycopeptide biosynthetic gene cluster that is predicted to encode the biosynthesis of a polysulfated glycopeptide congener, was recently cloned from DNA extracted directly from desert soil. This predicted glycopeptide gene cluster contains three closely related sulfotransferases (Teg12, -13, and -14) that sulfate teicoplanin-like glycopeptides at three unique sites. Here we report a series of structures: an apo structure of Teg12, Teg12 bound to the desulfated cosubstrate 3'-phosphoadenosine 5'-phosphate, and Teg12 bound to the teicoplanin aglycone. Teg12 appears to undergo a series of significant conformational rearrangements during glycopeptide recruitment, binding, and catalysis. Loop regions that exhibit the most conformational flexibility show the least sequence conservation between TEG sulfotransferases. Site-directed mutagenesis guided by our structural studies confirmed the importance of key catalytic residues as well as the importance of residues found throughout the conformationally flexible loop regions.

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