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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.

Author information

1
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.

Abstract

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.

PMID:
20361791
PMCID:
PMC2888265
DOI:
10.1021/bi100150v
[Indexed for MEDLINE]
Free PMC Article

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