7MQM

AAC(3)-IIIa in complex with CoA and gentamicin

7MQM の概要

• エントリーDOI: 10.2210/pdb7mqm/pdb
• 分子名称: Aminoglycoside N(3)-acetyltransferase III, COENZYME A, gentamicin C1, ... (5 entities in total)
• 機能のキーワード: antibiotic resistance, aminoglycoside, acetyltransferase, transferase
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 124956.48

構造登録者

Zielinski, M.,Berghuis, A.M. (登録日: 2021-05-05, 公開日: 2022-07-06, 最終更新日: 2024-11-20)

主引用文献

Zielinski, M.,Blanchet, J.,Hailemariam, S.,Berghuis, A.M.
Structural elucidation of substrate-bound aminoglycoside acetyltransferase (3)-IIIa.
Plos One, 17:e0269684-e0269684, 2022

PubMed Abstract: Canonical aminoglycosides are a large group of antibiotics, where the part of chemical diversity stems from the substitution of the neamine ring system on positions 5 and 6. Certain aminoglycoside modifying enzymes can modify a broad range of 4,5- and 4,6-disubstituted aminoglycosides, with some as many as 15. This study presents the structural and kinetic results describing a promiscuous aminoglycoside acetyltransferase AAC(3)-IIIa. This enzyme has been crystallized in ternary complex with coenzyme A and 4,5- and 4,6-disubstituted aminoglycosides. We have followed up this work with kinetic characterization utilizing a panel of diverse aminoglycosides, including a next-generation aminoglycoside, plazomicin. Lastly, we observed an alternative binding mode of gentamicin in the aminoglycoside binding site, which was proven to be a crystallographic artifact based on mutagenesis.

PubMed: 35921328
DOI: 10.1371/journal.pone.0269684

実験手法

X-RAY DIFFRACTION (1.6 Å)