5DCC

X-RAY CRYSTAL STRUCTURE OF a TEBIPENEM ADDUCT OF L,D TRANSPEPTIDASE 2 FROM MYCOBACTERIUM TUBERCULOSIS

5DCC の概要

• エントリーDOI: 10.2210/pdb5dcc/pdb
• 関連するPDBエントリー: 3TUR 5DC2 5DH7
• 分子名称: L,D-transpeptidase 2, (4S)-4-methyl-2,5,7-trioxoheptanoic acid, SULFATE ION, ... (8 entities in total)
• 機能のキーワード: l, d -transpeptidase, carbapenems tebipenem-adduct, transferase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 79323.56

構造登録者

Pan, Y.,Basta, L.,Lamichhane, G.,Bianchet, M.A. (登録日: 2015-08-23, 公開日: 2016-09-28, 最終更新日: 2024-10-23)

主引用文献

Bianchet, M.A.,Pan, Y.H.,Basta, L.A.B.,Saavedra, H.,Lloyd, E.P.,Kumar, P.,Mattoo, R.,Townsend, C.A.,Lamichhane, G.
Structural insight into the inactivation of Mycobacterium tuberculosis non-classical transpeptidase LdtMt2 by biapenem and tebipenem.
BMC Biochem., 18:8-8, 2017

PubMed Abstract: The carbapenem subclass of β-lactams is among the most potent antibiotics available today. Emerging evidence shows that, unlike other subclasses of β-lactams, carbapenems bind to and inhibit non-classical transpeptidases (L,D-transpeptidases) that generate 3 → 3 linkages in bacterial peptidoglycan. The carbapenems biapenem and tebipenem exhibit therapeutically valuable potencies against Mycobacterium tuberculosis (Mtb).

PubMed: 28545389
DOI: 10.1186/s12858-017-0082-4

実験手法

X-RAY DIFFRACTION (2.451 Å)