2W7Z
Structure of the pentapeptide repeat protein EfsQnr, a DNA gyrase inhibitor. Free amines modified by cyclic pentylation with glutaraldehyde.
Summary for 2W7Z
| Entry DOI | 10.2210/pdb2w7z/pdb |
| Descriptor | PENTAPEPTIDE REPEAT FAMILY PROTEIN, CHLORIDE ION (3 entities in total) |
| Functional Keywords | glutaraldehyde, gyrase inhibitor, cyclic pentylation, chemical modification, pentapeptide repeat protein, inhibitor |
| Biological source | ENTEROCOCCUS FAECALIS |
| Total number of polymer chains | 2 |
| Total formula weight | 50188.53 |
| Authors | Vetting, M.W.,Hegde, S.S.,Blanchard, J.S. (deposition date: 2009-01-06, release date: 2009-05-05, Last modification date: 2024-10-09) |
| Primary citation | Vetting, M.W.,Hegde, S.S.,Blanchard, J.S. Crystallization of a Pentapeptide-Repeat Protein by Reductive Cyclic Pentylation of Free Amines with Glutaraldehyde. Acta Crystallogr.,Sect.D, 65:462-, 2009 Cited by PubMed 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. PubMed: 19390151DOI: 10.1107/S0907444909008324 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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