3MGC

Teg12 Apo

Summary for 3MGC

• Entry DOI: 10.2210/pdb3mgc/pdb
• Related: 3MG9 3MGB
• Descriptor: Teg12, GLYCEROL, IMIDAZOLE, ... (5 entities in total)
• Functional Keywords: sulfotransferase, teicoplanin, antibiotic, environmental dna, paps, transferase
• Biological source: uncultured soil bacterium
• Total number of polymer chains: 2
• Total formula weight: 70586.45

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: 2023-09-06)

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, 49:4159-4168, 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 (2.91 Å)