Crystallization and preliminary X-ray diffraction analysis of full-length spr1814, a response regulator of Streptococcus pneumoniae, in complex with a phosphoryl analogue

Aekyung Park, Jae Soon Oh, Young Min Chi, Seong Weon Jeong

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Spr1814 of Streptococcus pneumoniae is a signal transduction response regulator belonging to the NarL/FixJ subfamily, which has a helix-turn-helix DNA-binding effector domain. To understand how the phosphorylation of the conserved aspartic acid residue induces conformational changes in spr1814 allowing binding to the target promoter, recombinant spr1814 expressed in Escherichia coli was crystallized with the phosphoryl analogue beryllium fluoride BeF3 <sup>-</sup> by the hanging-drop vapour-diffusion method. The crystals diffracted to 1.9 Å resolution and belonged to space group P21, with unit-cell parameters a = 40.2, b = 114.5, c = 50.1 Å, β = 92.1°. Structure determination by the SAD method using the bromine derivative 5-amino-2,4,6-tribromo-isophthalic acid (B3C) is under way.

Original languageEnglish
Pages (from-to)1428-1430
Number of pages3
JournalActa Crystallographica Section F:Structural Biology Communications
Volume70
DOIs
Publication statusPublished - 2014 Oct 1

Keywords

  • Spr1814
  • Streptococcus pneumoniae

ASJC Scopus subject areas

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

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