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

Ae Kyung Park; Jeong Hye Lee; Young Min Chi; Hyun Park

doi:10.1016/j.bbrc.2016.03.144

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

Ae Kyung Park, Jeong Hye Lee, Young Min Chi, Hyun Park

Research output: Contribution to journal › Article › peer-review

7 Citations (Scopus)

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 Å. 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 α4-β5-α5 interface, leading to the domain reorganization of spr1814, and this is achieved by a rotational change in the C-terminal DNA-binding domain.

Original language	English
Pages (from-to)	625-629
Number of pages	5
Journal	Biochemical and biophysical research communications
Volume	473
Issue number	2
DOIs	https://doi.org/10.1016/j.bbrc.2016.03.144
Publication status	Published - 2016 Apr 29

Bibliographical note

Funding Information:
We thank the staff at beamline 7A of the Pohang Light Source, Republic of Korea and beamline AR-NW12 of the Photon Factory, Japan for assistance during data collection. This work was supported by the Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science and Technology (grant No. 2011-0012059 ).

Publisher Copyright:
© 2016 Elsevier Inc.

Keywords

NarL subfamily
Phosphorylation
Response regulator
Streptococcus pneumoniae
Two-component system

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2016.03.144

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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. / Park, Ae Kyung; Lee, Jeong Hye; Chi, Young Min et al.
In: Biochemical and biophysical research communications, Vol. 473, No. 2, 29.04.2016, p. 625-629.

Research output: Contribution to journal › Article › peer-review

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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 {\AA}. 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 α4-β5-α5 interface, leading to the domain reorganization of spr1814, and this is achieved by a rotational change in the C-terminal DNA-binding domain.",

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author = "Park, {Ae Kyung} and Lee, {Jeong Hye} and Chi, {Young Min} and Hyun Park",

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AU - Chi, Young Min

AU - Park, Hyun

N1 - Funding Information: We thank the staff at beamline 7A of the Pohang Light Source, Republic of Korea and beamline AR-NW12 of the Photon Factory, Japan for assistance during data collection. This work was supported by the Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science and Technology (grant No. 2011-0012059 ). Publisher Copyright: © 2016 Elsevier Inc.

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AB - 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 Å. 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 α4-β5-α5 interface, leading to the domain reorganization of spr1814, and this is achieved by a rotational change in the C-terminal DNA-binding domain.

KW - NarL subfamily

KW - Phosphorylation

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KW - Streptococcus pneumoniae

KW - Two-component system

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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

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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