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 |
|---|---|
| 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 |
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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 journal › Article
}
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
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
UR - http://www.scopus.com/inward/record.url?scp=84876808041&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84876808041&partnerID=8YFLogxK
U2 - 10.1016/j.bbrc.2013.03.065
DO - 10.1016/j.bbrc.2013.03.065
M3 - Article
VL - 434
SP - 65
EP - 69
JO - The BMJ
JF - The BMJ
SN - 0730-6512
IS - 1
ER -