TY - JOUR
T1 - Crystal structure of the response regulator spr1814 from Streptococcus pneumoniae reveals unique interdomain contacts among NarL family proteins
AU - Park, Ae Kyung
AU - Moon, Jin Ho
AU - Oh, Jae Soon
AU - Lee, Ki Seog
AU - Chi, Young Min
N1 - Funding Information:
We thank the staff at beamline 4A of Pohang Light Source, South Korea for assistance during data collection. This work was supported by a Korea Research Foundation Grant ( KRF-2007-359-C00026 ) funded by the Korean Government (MOEHRD).
Copyright:
Copyright 2013 Elsevier B.V., All rights reserved.
PY - 2013/4/26
Y1 - 2013/4/26
N2 - 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.
AB - 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.
KW - Helix-turn-helix fold
KW - NarL subfamily
KW - Response regulators
KW - Streptococcus pneumoniae
KW - Two-component phosphotransfer pathways
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U2 - 10.1016/j.bbrc.2013.03.065
DO - 10.1016/j.bbrc.2013.03.065
M3 - Article
C2 - 23545256
AN - SCOPUS:84876808041
VL - 434
SP - 65
EP - 69
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -