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 language | English |
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Pages (from-to) | 65-69 |
Number of pages | 5 |
Journal | Biochemical and biophysical research communications |
Volume | 434 |
Issue number | 1 |
DOIs | |
Publication status | Published - 2013 Apr 26 |
Keywords
- Helix-turn-helix fold
- NarL subfamily
- Response regulators
- Streptococcus pneumoniae
- Two-component phosphotransfer pathways
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology