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

Authors
Park, Ae KyungMoon, Jin HoOh, Jae SoonLee, Ki SeogChi, Young Min
Issue Date
26-4월-2013
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Keywords
Two-component phosphotransfer pathways; Response regulators; NarL subfamily; Helix-turn-helix fold; Streptococcus pneumoniae
Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.434, no.1, pp.65 - 69
Indexed
SCIE
SCOPUS
Journal Title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume
434
Number
1
Start Page
65
End Page
69
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/103474
DOI
10.1016/j.bbrc.2013.03.065
ISSN
0006-291X
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 angstrom 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. (C) 2013 Elsevier Inc. All rights reserved.
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생명과학대학 (생명공학부)
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