2TDT

COMPLEX OF TETRAHYDRODIPICOLINATE N-SUCCINYLTRANSFERASE WITH 2-AMINOPIMELATE AND COENZYME A

2TDT の概要

• エントリーDOI: 10.2210/pdb2tdt/pdb
• 分子名称: TETRAHYDRODIPICOLINATE N-SUCCINYLTRANSFERASE, COENZYME A, (2S)-2-aminoheptanedioic acid, ... (4 entities in total)
• 機能のキーワード: acyltransferase, lysine 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: 1
• 化学式量合計: 30861.71

構造登録者

Beaman, T.W.,Blanchard, J.S.,Roderick, S.L. (登録日: 1998-05-05, 公開日: 1998-10-14, 最終更新日: 2024-05-22)

主引用文献

Beaman, T.W.,Blanchard, J.S.,Roderick, S.L.
The conformational change and active site structure of tetrahydrodipicolinate N-succinyltransferase.
Biochemistry, 37:10363-10369, 1998

PubMed Abstract: Tetrahydrodipicolinate (THDP) N-succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to L-2-(succinylamino)-6-oxopimelate and CoA. This reaction represents the committed step of the succinylase branch of the diaminopimelate/L-lysine biosynthetic pathway by which many bacteria synthesize meso-diaminopimelate, a component of peptidoglycan, and L-lysine from L-aspartate. The crystal structures of THDP succinyltransferase in complex with the substrate/cofactor pairs L-2-aminopimelate/coenzyme A and L-2-amino-6-oxopimelate/coenzyme A have been determined and refined to 2.0 A resolution. The active site of the enzyme is a long narrow groove located at the interface between two left-handed parallel beta-helix (LbetaH) structural domains of the trimeric enzyme. On binding the amino acid acceptor and cofactor, this groove is covered by residues from the C-terminus of one subunit and a flexible loop excluded from the LbetaH domain of an adjacent subunit to form a tunnel. This conformational change is directly related to interactions between the enzyme and the bound amino acid substrate and cofactor and serves to shield the ligands from bulk solvent and to orient the nucleophilic amino group of the amino acid acceptor toward the mercaptoethylamine group of the cofactor.

PubMed: 9671504
DOI: 10.1021/bi980759b

実験手法

X-RAY DIFFRACTION (2 Å)