1M4D

Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis-Complex with Coenzyme A and Tobramycin

1M4D の概要

• エントリーDOI: 10.2210/pdb1m4d/pdb
• 関連するPDBエントリー: 1M44 1M4G 1M4I
• 分子名称: Aminoglycoside 2'-N-acetyltransferase, TOBRAMYCIN, COENZYME A, ... (5 entities in total)
• 機能のキーワード: coa binding motif, 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: 43104.67

構造登録者

Vetting, M.W.,Hegde, S.S.,Javid-Majd, F.,Blanchard, J.S.,Roderick, S.L. (登録日: 2002-07-02, 公開日: 2002-08-28, 最終更新日: 2024-02-14)

主引用文献

Vetting, M.W.,Hegde, S.S.,Javid-Majd, F.,Blanchard, J.S.,Roderick, S.L.
Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme A and aminoglycoside substrates.
Nat.Struct.Biol., 9:653-658, 2002

PubMed Abstract: AAC(2')-Ic catalyzes the coenzyme A (CoA)-dependent acetylation of the 2' hydroxyl or amino group of a broad spectrum of aminoglycosides. The crystal structure of the AAC(2')-Ic from Mycobacterium tuberculosis has been determined in the apo enzyme form and in ternary complexes with CoA and either tobramycin, kanamycin A or ribostamycin, representing the first structures of an aminoglycoside acetyltransferase bound to a drug. The overall fold of AAC(2')-Ic places it in the GCN5-related N-acetyltransferase (GNAT) superfamily. Although the physiological function of AAC(2')-Ic is uncertain, a structural analysis of these high-affinity aminoglycoside complexes suggests that the enzyme may acetylate a key biosynthetic intermediate of mycothiol, the major reducing agent in mycobacteria, and participate in the regulation of cellular redox potential.

PubMed: 12161746
DOI: 10.1038/nsb830

実験手法

X-RAY DIFFRACTION (1.8 Å)