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Crystal structure of receiver domain of putative NarL family response regulator spr1814 from Streptococcus pneumoniae in the absence and presence of the phosphoryl analog beryllofluoride

Authors
Park, Ae KyungMoon, Jin HoLee, Ki SeogChi, Young Min
Issue Date
4-5월-2012
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Keywords
Two-component phosphotransfer pathways; Response regulator; Receiver domain; Phosphoryl analog beryllofluoride
Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.421, no.2, pp.403 - 407
Indexed
SCIE
SCOPUS
Journal Title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume
421
Number
2
Start Page
403
End Page
407
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/108449
DOI
10.1016/j.bbrc.2012.04.035
ISSN
0006-291X
Abstract
Spr1814 of Streptococcus pneumoniae is a putative response regulator (RR) that has four-helix helix-turn-helix DNA-binding domain and belongs to the NarL family. The prototypical RR contains two domains, an N-terminal receiver domain linked to a variable effector domain. The receiver domain functions as a phosphorylation-activated switch and contains the typical doubly wound five-stranded alpha/beta fold. Here, we report the crystal structure of the receiver domain of spr1814 (spr1814(R)) determined in the absence and presence of beryllofluoride as a phosphoryl analog. Based on the overall structure, spr1814(R) was shown to contain the typical fold similar with other structures of the receiver domain; however, an additional linker region connecting the receiver and DNA-binding domain was inserted into the dimer interface of spr1814(R), resulting in the formation of unique dimer interface. Upon phosphorylation, the conformational change of the linker region was observed and this suggests that domain rearrangement between the receiver domain and effector domain could occur in full-length spr1814. (C) 2012 Elsevier Inc. All rights reserved.
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생명과학대학 (생명공학부)
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