Skip to main content
padlock icon - secure page this page is secure

Crystallization and preliminary crystal structure analysis of the ligand‐binding domain of PqsR (MvfR), the

Buy Article:

$52.00 + tax (Refund Policy)

The opportunistic bacterial pathogen Pseudomonas aeruginosa employs three transcriptional regulators, LasR, RhlR and PqsR, to control the transcription of a large subset of its genes in a cell‐density‐dependent process known as quorum sensing. Here, the recombinant production, crystallization and structure solution of the ligand‐binding domain of PqsR (MvfR), the LysR‐type transcription factor that responds to the Pseudomonas quinolone signal (PQS), a quinolone‐based quorum‐sensing signal that is unique to P. aeruginosa and possibly a small number of other bacteria, is reported. PqsR regulates the expression of many virulence genes and may therefore be an interesting drug target. The ligand‐binding domain (residues 91–319) was produced as a fusion with SUMO, and hexagonal‐shaped crystals of purified PqsR_91–319 were obtained using the vapour‐diffusion method. Crystallization in the presence of a PQS precursor allowed data collection to 3.25 Å resolution on a synchrotron beamline, and initial phases have been obtained using single‐wavelength anomalous diffraction data from seleno‐l‐methionine‐labelled crystals, revealing the space group to be P6522, with unit‐cell parameters a = b = 116–120, c = 115–117 Å.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Document Type: Research Article

Publication date: September 1, 2012

  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
X
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more