1B87

CRYSTAL STRUCTURE OF AN AMINOGLYCOSIDE 6'-N-ACETYLTRANSFERASE

Summary for 1B87

• Entry DOI: 10.2210/pdb1b87/pdb
• Descriptor: PROTEIN (AMINOGLYCOSIDE N6'-ACETYLTRANSFERASE TYPE 1), ACETYL COENZYME *A (3 entities in total)
• Functional Keywords: aminoglycoside 6'-n-acetyltransferase, antibiotic resistance, acetyl coenzyme a, transferase
• Biological source: Enterococcus faecium
• Total number of polymer chains: 1
• Total formula weight: 21411.64

Authors

Wybenga-Groot, L.E.,Berghuis, A.M. (deposition date: 1999-02-09, release date: 1999-06-30, Last modification date: 2023-12-27)

Primary citation

Wybenga-Groot, L.E.,Draker, K.,Wright, G.D.,Berghuis, A.M.
Crystal structure of an aminoglycoside 6'-N-acetyltransferase: defining the GCN5-related N-acetyltransferase superfamily fold.
Structure Fold.Des., 7:497-507, 1999

PubMed Abstract: The predominant mechanism of antibiotic resistance employed by pathogenic bacteria against the clinically used aminoglycosides is chemical modification of the drug. The detoxification reactions are catalyzed by enzymes that promote either the phosphorylation, adenylation or acetylation of aminoglycosides. Structural studies of these aminoglycoside-modifying enzymes may assist in the development of therapeutic agents that could circumvent antibiotic resistance. In addition, such studies may shed light on the development of antibiotic resistance and the evolution of different enzyme classes.

PubMed: 10378269
DOI: 10.1016/S0969-2126(99)80066-5

Experimental method

X-RAY DIFFRACTION (2.7 Å)