Open AccessPurification, crystallization and preliminary X‐ray analysis of the aminoglycoside‐6′‐acetyltransferase AAC(6′)‐Im
Author(s) -
Toth Marta,
Vakulenko Sergei B.,
Smith Clyde A.
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112007117
Subject(s) - escherichia coli , acetyltransferase , acetyltransferases , aminoglycoside , kanamycin , enzyme , molecular replacement , chemistry , crystallization , acetylation , biochemistry , transferase , crystallography , gene , antibiotics , stereochemistry , organic chemistry
Bacterial resistance to the aminoglycoside antibiotics is primarily the result of enzymatic deactivation of the drugs. The aminoglycoside N ‐acetyltransferases (AACs) are a large family of bacterial enzymes that are responsible for coenzyme‐A‐facilitated acetylation of aminoglycosides. The gene encoding one of these enzymes, AAC(6′)‐Im, has been cloned and the protein (comprising 178 amino‐acid residues) was expressed in Escherichia coli , purified and crystallized as the kanamycin complex. Synchrotron diffraction data to approximately 2.0 Å resolution were collected from a crystal of this complex on beamline BL12‐2 at SSRL (Stanford, California, USA). The crystals belonged to the hexagonal space group P 6 5 , with approximate unit‐cell parameters a = 107.75, c = 37.33 Å, and contained one molecule in the asymmetric unit. Structure determination is under way using molecular replacement.