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

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 A resolution using synchrotron radiation and the crystals belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 46.91, b = 71.38, c = 117.73 A. Assuming the presence of a dimer in the asymmetric unit, this corresponds to a V(M) of 2.21 A(3) Da(-1).

SUBMITTER: Park AK

PROVIDER: S-EPMC2705646 | biostudies-literature | 2009 Jul

REPOSITORIES: biostudies-literature

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

Park Ae Kyung AK Bong Seung Min SM Moon Jin Ho JH Chi Young Min YM

Acta crystallographica. Section F, Structural biology and crystallization communications 20090627 Pt 7

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 A resolution using synchrotron radiation and the crystals belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell paramete ...[more]

PMID: 19574651

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