Journal article
Crystal structure of an aminoglycoside 6'-N-acetyltransferase: defining the GCN5-related N-acetyltransferase superfamily fold
Abstract
BACKGROUND: 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 …
Authors
Wybenga-Groot LE; Draker K; Wright GD; Berghuis AM
Journal
Structure (London, England: 1993), Vol. 7, No. 5, pp. 497–507
Publication Date
May 1999
ISSN
0969-2126
Fields of Research (FoR)
Medical Subject Headings (MeSH)
Acetyl Coenzyme AAcetylationAcetyltransferasesAmino Acid SequenceCrystallography, X-RayDNA-Binding ProteinsFungal ProteinsHistone AcetyltransferasesModels, MolecularMolecular Sequence DataProtein ConformationProtein FoldingProtein KinasesSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSubstrate Specificity