Journal article
The COOH terminus of aminoglycoside phosphotransferase (3')-IIIa is critical for antibiotic recognition and resistance
Abstract
The aminoglycoside phosphotransferases (APHs) are widely distributed among pathogenic bacteria and are employed to covalently modify, and thereby detoxify, the clinically relevant aminoglycoside antibiotics. The crystal structure for one of these aminoglycoside kinases, APH(3')-IIIa, has been determined in complex with ADP and analysis of the electrostatic surface potential indicates that there is a large anionic depression present adjacent to …
Authors
Thompson PR; Schwartzenhauer J; Hughes DW; Berghuis AM; Wright GD
Journal
The Journal of Biological Chemistry, Vol. 274, No. 43, pp. 30697–30706
Publication Date
October 22, 1999
ISSN
0021-9258
Fields of Research (FoR)
Medical Subject Headings (MeSH)
Amino Acid SequenceAminoglycosidesAnti-Bacterial AgentsBinding SitesCarbohydrate SequenceConserved SequenceEscherichia coliKanamycin KinaseMicrobial Sensitivity TestsModels, MolecularMolecular ConformationMolecular Sequence DataMolecular StructureMutagenesis, Site-DirectedNuclear Magnetic Resonance, BiomolecularPhenylalaninePolymerase Chain ReactionProtein Structure, SecondaryRecombinant ProteinsSequence DeletionStatic Electricity