5E96

Crystal structure of aminoglycoside 6'-acetyltransferase type Ii

5E96 の概要

• エントリーDOI: 10.2210/pdb5e96/pdb
• 関連するPDBエントリー: 1B87 1N71
• 分子名称: Aminoglycoside 6'-acetyltransferase, PHOSPHATE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: gnat, acetyltransferase, aminoglycoside resistance, transferase
• 由来する生物種: Enterococcus faecium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20672.03

構造登録者

Berghuis, A.M.,Burk, D.L.,Baettig, O.M.,Shi, K. (登録日: 2015-10-14, 公開日: 2016-07-06, 最終更新日: 2023-09-27)

主引用文献

Baettig, O.M.,Shi, K.,Yachnin, B.J.,Burk, D.L.,Berghuis, A.M.
Comprehensive characterization of ligand-induced plasticity changes in a dimeric enzyme.
Febs J., 283:3029-3038, 2016

PubMed Abstract: An enzyme's inherent structural plasticity is frequently associated with substrate binding, yet detailed structural characterization of flexible proteins remains challenging. This study employs complementary biophysical methods to characterize the partially unfolded structure of substrate-free AAC(6')-Ii, an N-acetyltransferase of the GCN5-related N-acetyltransferase (GNAT) superfamily implicated in conferring broad-spectrum aminoglycoside resistance on Enterococcus faecium. The X-ray crystal structure of AAC(6')-Ii is analyzed to identify relative motions of the structural elements that constitute the dimeric enzyme. Comparison with the previously elucidated crystal structure of AAC(6')-Ii with acetyl coenzyme A (AcCoA) reveals conformational changes that occur upon substrate binding. Our understanding of the enzyme's structural plasticity is further refined with small-angle X-ray scattering and circular dichroism analyses, which together reveal how flexible structural elements impact dimerization and substrate binding. These results clarify the extent of unfolding that AAC(6')-Ii undergoes in the absence of AcCoA and provide a structural connection to previously observed allosteric cooperativity of this enzyme.

PubMed: 27333541
DOI: 10.1111/febs.13788

実験手法

X-RAY DIFFRACTION (2.1 Å)