Structural highlights
Publication Abstract from PubMed
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 1.7A 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.
Crystal structure of the response regulator spr1814 from Streptococcus pneumoniae reveals unique interdomain contacts among NarL family proteins.,Park AK, Moon JH, Oh JS, Lee KS, Chi YM Biochem Biophys Res Commun. 2013 Apr 26;434(1):65-9. doi:, 10.1016/j.bbrc.2013.03.065. Epub 2013 Mar 30. PMID:23545256[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Park AK, Moon JH, Oh JS, Lee KS, Chi YM. Crystal structure of the response regulator spr1814 from Streptococcus pneumoniae reveals unique interdomain contacts among NarL family proteins. Biochem Biophys Res Commun. 2013 Apr 26;434(1):65-9. doi:, 10.1016/j.bbrc.2013.03.065. Epub 2013 Mar 30. PMID:23545256 doi:10.1016/j.bbrc.2013.03.065
