3NIB
Teg14 Apo
Summary for 3NIB
| Entry DOI | 10.2210/pdb3nib/pdb |
| Descriptor | Teg14, 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | antibiotic transferase, transferase |
| Biological source | uncultured soil bacterium |
| Total number of polymer chains | 1 |
| Total formula weight | 34869.45 |
| Authors | Bick, M.J.,Banik, J.J.,Darst, S.A.,Brady, S.F. (deposition date: 2010-06-15, release date: 2010-12-08, Last modification date: 2024-11-06) |
| Primary citation | Bick, M.J.,Banik, J.J.,Darst, S.A.,Brady, S.F. The 2.7 A resolution structure of the glycopeptide sulfotransferase Teg14 Acta Crystallogr.,Sect.D, 66:1278-1286, 2010 Cited by PubMed Abstract: The TEG gene cluster was recently isolated from an environmental DNA library and is predicted to encode the biosynthesis of a polysulfated glycopeptide congener. Three closely related sulfotransferases found in the TEG gene cluster (Teg12, Teg13 and Teg14) have been shown to sulfate the teicoplanin aglycone at three unique sites. Crystal structures of the first sulfotransferase from the TEG cluster, Teg12, in complex with the teicoplanin aglycone and its desulfated cosubstrate PAP have recently been reported [Bick et al. (2010), Biochemistry, 49, 4159-4168]. Here, the 2.7 Å resolution crystal structure of the apo form of Teg14 is reported. Teg14 sulfates the hydroxyphenylglycine at position 4 in the teicoplanin aglycone. The Teg14 structure is discussed and is compared with those of other bacterial 3'-phosphoadenosine 5'-phosphosulfate-dependent sulfotransferases. PubMed: 21123867DOI: 10.1107/S0907444910036681 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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