| Literature DB >> 19390151 |
Matthew W Vetting1, Subray S Hegde, John S Blanchard.
Abstract
The pentapeptide-repeat protein EfsQnr from Enterococcus faecalis protects DNA gyrase from inhibition by fluoroquinolones. EfsQnr was cloned and purified to homogeneity, but failed to produce diffraction-quality crystals in initial crystallization screens. Treatment of EfsQnr with glutaraldehyde and the strong reducing agent borane-dimethylamine resulted in a derivatized protein which produced crystals that diffracted to 1.6 A resolution; their structure was subsequently determined by single-wavelength anomalous dispersion. Analysis of the derivatized protein using Fourier transform ion cyclotron resonance mass spectrometry indicated a mass increase of 68 Da per free amino group. Electron-density maps about a limited number of structurally ordered lysines indicated that the modification was a cyclic pentylation of free amines, producing piperidine groups.Entities:
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Year: 2009 PMID: 19390151 PMCID: PMC2672816 DOI: 10.1107/S0907444909008324
Source DB: PubMed Journal: Acta Crystallogr D Biol Crystallogr ISSN: 0907-4449