Structural characterization of the full-length response regulator spr1814 in complex with a phosphate analogue reveals a novel conformational plasticity of the linker region

Ae Kyung Park, Jeong Hye Lee, Young Min Chi, Hyun Park

Research output: Contribution to journalArticle

5 Citations (Scopus)


Spr1814 of Streptococcus pneumoniae is a response regulator (RR) that belongs to the NarL/FixJ subfamily and has a four-helix helix-turn-helix DNA-binding domain. Here, the X-ray crystal structure of the full-length spr1814 in complex with a phosphate analogue beryllium fluoride (BeF3-) was determined at 2.0 Å. This allows for a structural comparison with the previously reported full-length unphosphorylated spr1814. The phosphorylation of conserved aspartic acid residue of N-terminal receiver domain triggers a structural perturbation at the α4-β5-α5 interface, leading to the domain reorganization of spr1814, and this is achieved by a rotational change in the C-terminal DNA-binding domain.

Original languageEnglish
Pages (from-to)625-629
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - 2016 Apr 29



  • NarL subfamily
  • Phosphorylation
  • Response regulator
  • Streptococcus pneumoniae
  • Two-component system

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

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