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TitleThe molecular mechanisms of allosteric mutations impairing MepR repressor function in multidrug-resistant strains of Staphylococcus aureus.
Journal, issue, pagesMBio, Vol. 4, Page e00528-e00513, Year 2013
Publish dateJun 18, 2013 (structure data deposition date)
AuthorsBirukou, I. / Tonthat, N.K. / Seo, S.M. / Schindler, B.D. / Kaatz, G.W. / Brennan, R.G.
External linksMBio / PubMed:23982071
MethodsX-ray diffraction
Resolution1.6 - 3.45 Å
Structure data

PDB-4l9j:
Crystal structure of S. aureus MepR in DNA-binding conformation
Method: X-RAY DIFFRACTION / Resolution: 3.45 Å

PDB-4l9n:
Crystal structure of MepR A103V mutant from multidrug resistant S. aureus clinical isolate
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-4l9t:
Crystal structure of MepR F27L mutant from multidrug resistant S. aureus clinical isolate
Method: X-RAY DIFFRACTION / Resolution: 1.794 Å

PDB-4l9v:
Crystal structure of Se-Met derivative MepR F27L mutant from multidrug resistant S. aureus clinical isolate
Method: X-RAY DIFFRACTION / Resolution: 2.374 Å

PDB-4ld5:
Crystal structure of MepR Q18P mutant from multidrug resistant S. aureus clinical isolate
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • staphylococcus aureus (bacteria)
KeywordsTRANSCRIPTION / winged helix-turn-helix / wHTH / transcription repressor / wing-helix-turn-helix / transcription repression / multidrug resistance

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