3NIB

Teg14 Apo

3NIB の概要

• エントリーDOI: 10.2210/pdb3nib/pdb
• 分子名称: Teg14, 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: antibiotic transferase, transferase
• 由来する生物種: uncultured soil bacterium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34869.45

構造登録者

Bick, M.J.,Banik, J.J.,Darst, S.A.,Brady, S.F. (登録日: 2010-06-15, 公開日: 2010-12-08, 最終更新日: 2024-11-06)

主引用文献

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

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: 21123867
DOI: 10.1107/S0907444910036681

実験手法

X-RAY DIFFRACTION (2.7 Å)