3MG9

Teg 12 Binary Structure Complexed with the Teicoplanin Aglycone

Summary for 3MG9

• Entry DOI: 10.2210/pdb3mg9/pdb
• Related: 2WDX 3MGB 3MGC
• Related PRD ID: PRD_000210
• Descriptor: TEG12, TEICOPLANIN AGLYCONE, FORMIC ACID, ... (5 entities in total)
• Functional Keywords: sulfotransferase, glyopeptide, antibiotic, transferase-antibiotic complex, transferase/antibiotic
• Biological source: UNCULTURED SOIL BACTERIUM; More
• Total number of polymer chains: 3
• Total formula weight: 34786.47

Authors

Bick, M.J.,Banik, J.J.,Darst, S.A.,Brady, S.F. (deposition date: 2010-04-05, release date: 2010-06-09, Last modification date: 2023-11-22)

Primary citation

Bick, M.J.,Banik, J.J.,Darst, S.A.,Brady, S.F.
Crystal Structures of the Glycopeptide Sulfotransferase Teg12 in a Complex with the Teicoplanin Aglycone.
Biochemistry, 49:4159-, 2010

PubMed 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.

PubMed: 20361791
DOI: 10.1021/BI100150V

Experimental method

X-RAY DIFFRACTION (2.27 Å)