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Structural characterization of the full-length response regulator spr1814 in complex with a phosphate analogue reveals a novel conformational plasticity of the linker region

Authors
Park, Ae KyungLee, Jeong HyeChi, Young MinPark, Hyun
Issue Date
29-4월-2016
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Keywords
Two-component system; Response regulator; NarL subfamily; Phosphorylation; Streptococcus pneumoniae
Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.473, no.2, pp.625 - 629
Indexed
SCIE
SCOPUS
Journal Title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume
473
Number
2
Start Page
625
End Page
629
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/88884
DOI
10.1016/j.bbrc.2016.03.144
ISSN
0006-291X
Abstract
Spr1814 of Streptococcus pneumoniae is a response regulator (RR) that belongs to the NarL/FixJ subfamily and has a four-helix helix-turn-helix DNA-binding domain. Here, the X-ray crystal structure of the full-length spr1814 in complex with a phosphate analogue beryllium fluoride (BeF3-) was determined at 2.0 angstrom. This allows for a structural comparison with the previously reported full-length unphosphorylated spr1814. The phosphorylation of conserved aspartic acid residue of N-terminal receiver domain triggers a structural perturbation at the alpha 4-beta 5-alpha 5 interface, leading to the domain reorganization of spr1814, and this is achieved by a rotational change in the C-terminal DNA-binding domain. (C) 2016 Elsevier Inc. All rights reserved.
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생명과학대학 (생명공학부)
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