1TDT

THREE-DIMENSIONAL STRUCTURE OF TETRAHYDRODIPICOLINATE-N-SUCCINYLTRANSFERASE

1TDT の概要

• エントリーDOI: 10.2210/pdb1tdt/pdb
• 分子名称: TETRAHYDRODIPICOLINATE-N-SUCCINYLTRANSFERASE (2 entities in total)
• 機能のキーワード: transferase, succinyltransferase, lysine metabolism, hexapeptide transferase, cell wall biosynthesis
• 由来する生物種: Mycobacterium bovis
• 細胞内の位置: Cytoplasm: P56220
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 84747.17

構造登録者

Beaman, T.W.,Binder, D.W.,Blanchard, J.S.,Roderick, S.L. (登録日: 1996-11-19, 公開日: 1997-06-05, 最終更新日: 2024-02-14)

主引用文献

Beaman, T.W.,Binder, D.A.,Blanchard, J.S.,Roderick, S.L.
Three-dimensional structure of tetrahydrodipicolinate N-succinyltransferase.
Biochemistry, 36:489-494, 1997

PubMed Abstract: The conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA is catalyzed by tetrahydrodipicolinate N-succinyltransferase and is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The X-ray crystal structure of THDP succinyltransferase has been determined to 2.2 A resolution and has been refined to a crystallographic R-factor of 17.0%. The enzyme is trimeric and displays the left-handed parallel beta-helix (L beta H) structural motif encoded by the "hexapeptide repeat" amino acid sequence motif [Raetz, C.R.H., & Roderick, S.L. (1995) Science 270, 997-1000]. The approximate location of the active site of THDP succinyltransferase is suggested by the proximity of binding sites for two inhibitors: p-(chloromercuri)benzenesulfonic acid and cobalt ion, both of which bind to the L beta H domain.

PubMed: 9012664
DOI: 10.1021/bi962522q

実験手法

X-RAY DIFFRACTION (2.2 Å)