Crystal structure of the response regulator spr1814 from Streptococcus pneumoniae reveals unique interdomain contacts among NarL family proteins

Ae Kyung Park, Jin Ho Moon, Jae Soon Oh, Ki Seog Lee, Young Min Chi

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Spr1814 belongs to the NarL/FixJ subfamily of signal transduction response regulators (RR), and has been predicted to regulate the neighboring ABC transporter, which translocates antibiotic molecules in Streptococcus pneumoniae. Here, we report the crystal structure of full-length unphosphorylated spr1814 at 1.7. Å resolution. The asymmetric unit contains two spr1814 molecules, which display very different conformations. Through comparisons with other RRs structures, we concluded that one molecule adopts a general inactive conformation, whereas the other molecule adopts an intermediate conformation. The superposition of each molecule showed that rotational change of the effector domain occurred in intermediate conformational state, implying that domain rearrangement could occur upon phosphorylation.

Original languageEnglish
Pages (from-to)65-69
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume434
Issue number1
DOIs
Publication statusPublished - 2013 Apr 26

Fingerprint

ATP-Binding Cassette Transporters
Streptococcus pneumoniae
Signal Transduction
Crystal structure
Phosphorylation
Anti-Bacterial Agents
Molecules
Conformations
Proteins
Signal transduction

Keywords

  • Helix-turn-helix fold
  • NarL subfamily
  • Response regulators
  • Streptococcus pneumoniae
  • Two-component phosphotransfer pathways

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

Cite this

Crystal structure of the response regulator spr1814 from Streptococcus pneumoniae reveals unique interdomain contacts among NarL family proteins. / Park, Ae Kyung; Moon, Jin Ho; Oh, Jae Soon; Lee, Ki Seog; Chi, Young Min.

In: Biochemical and Biophysical Research Communications, Vol. 434, No. 1, 26.04.2013, p. 65-69.

Research output: Contribution to journalArticle

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