7BXZ

Crystal structure of the aminoglycoside 6'-N-acetyltransferase from Enterococcus faecium

Summary for 7BXZ

• Entry DOI: 10.2210/pdb7bxz/pdb
• Descriptor: Aminoglycoside 6'-N-acetyltransferase (2 entities in total)
• Functional Keywords: aminoglycoside acetyltransferase, enterococcus faecium, acetyl-coa, transferase
• Biological source: Enterococcus faecium
• Total number of polymer chains: 3
• Total formula weight: 62100.64

Authors

Kwon, S.,Park, H.H. (deposition date: 2020-04-21, release date: 2020-08-12, Last modification date: 2023-11-29)

Primary citation

Jang, H.,Kwon, S.,Jeong, C.S.,Lee, C.W.,Hwang, J.,Jung, K.H.,Lee, J.H.,Park, H.H.
Structural analysis of a novel substrate-free form of the aminoglycoside 6'-N-acetyltransferase from Enterococcus faecium.
Acta Crystallogr.,Sect.F, 76:364-371, 2020

PubMed Abstract: 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.

PubMed: 32744248
DOI: 10.1107/S2053230X20009735

Experimental method

X-RAY DIFFRACTION (2.502 Å)