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 Kyung; Lee, Jeong Hye; Chi, Young Min; Park, 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.
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - Graduate School > Department of Biosystems and Biotechnology > 1. Journal Articles
![qrcode](https://api.qrserver.com/v1/create-qr-code/?size=55x55&data=https://scholar.korea.ac.kr/handle/2021.sw.korea/88884)
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.