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Structural analysis of a novel substrate‐free form of the aminoglycoside 6′‐ N ‐acetyltransferase from Enterococcus faecium
Author(s) -
Jang Hyunseok,
Kwon Sunghark,
Jeong Chang-Sook,
Lee Chang Woo,
Hwang Jisub,
Jung Kyoung Ho,
Lee Jun Hyuck,
Park Hyun Ho
Publication year - 2020
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x20009735
Subject(s) - aminoglycoside , enterococcus faecium , acetyltransferases , acetyltransferase , chemistry , enzyme , acetylation , stereochemistry , n acetyltransferase , transferase , substrate (aquarium) , mechanism of action , biochemistry , antibiotics , biology , in vitro , ecology , gene
Aminoglycoside acetyltransferases (AACs) catalyze the transfer of an acetyl group between acetyl‐CoA and an aminoglycoside, producing CoA and an acetylated aminoglycoside. AAC(6′)‐Ii enzymes target the amino group linked to the 6′ C atom in an aminoglycoside. Several structures of the AAC(6′)‐Ii from Enterococcus faecium [Ef‐AAC(6′)‐Ii] have been reported to date. However, the detailed mechanism of its enzymatic function remains elusive. In this study, the crystal structure of Ef‐AAC(6′)‐Ii was determined in a novel substrate‐free form. Based on structural analysis, it is proposed that Ef‐AAC(6′)‐Ii sequentially undergoes conformational selection and induced fit for substrate binding. These results therefore provide a novel viewpoint on the mechanism of action of Ef‐AAC(6′)‐Ii.