Crystallization and preliminary X-ray crystallographic studies of DesR, a thermosensing response regulator in a two-component signalling system from Streptococcus pneumoniae

Ae Kyung Park, Seung Min Bong, Jin Ho Moon, Young Min Chi

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

The response regulator DesR, which activates the transcription of the des gene by binding to a regulatory region, is essential for controlling the fluidity of membrane phospholipids. DesR from Streptococcus pneumoniae was overexpressed in Escherichia coli. The protein was purified and crystallized for structural analysis. Diffraction data were collected to 1.7 Å resolution using synchrotron radiation and the crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 46.91, b = 71.38, c = 117.73 Å. Assuming the presence of a dimer in the asymmetric unit, this corresponds to a V M of 2.21 Å 3 Da -1.

Original languageEnglish
Pages (from-to)727-729
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume65
Issue number7
DOIs
Publication statusPublished - 2009 Aug 10

Fingerprint

Thermosensing
streptococcus
pneumonia
Synchrotrons
Membrane Fluidity
Fluidity
Nucleic Acid Regulatory Sequences
regulators
Transcription
Escherichia
Crystallization
Streptococcus pneumoniae
Synchrotron radiation
structural analysis
Structural analysis
genes
Dimers
Escherichia coli
Phospholipids
synchrotron radiation

Keywords

  • Fatty-acid desaturation
  • Response regulators
  • Two-component systems

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

Cite this

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abstract = "The response regulator DesR, which activates the transcription of the des gene by binding to a regulatory region, is essential for controlling the fluidity of membrane phospholipids. DesR from Streptococcus pneumoniae was overexpressed in Escherichia coli. The protein was purified and crystallized for structural analysis. Diffraction data were collected to 1.7 {\AA} resolution using synchrotron radiation and the crystals belonged to the orthorhombic space group P212121, with unit-cell parameters a = 46.91, b = 71.38, c = 117.73 {\AA}. Assuming the presence of a dimer in the asymmetric unit, this corresponds to a V M of 2.21 {\AA} 3 Da -1.",
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AU - Chi, Young Min

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