Crystallization and preliminary X-ray diffraction analysis of full-length spr1814, a response regulator of Streptococcus pneumoniae, in complex with a phosphoryl analogue

Aekyung Park, Jae Soon Oh, Young Min Chi, Seong Weon Jeong

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Spr1814 of Streptococcus pneumoniae is a signal transduction response regulator belonging to the NarL/FixJ subfamily, which has a helix-turn-helix DNA-binding effector domain. To understand how the phosphorylation of the conserved aspartic acid residue induces conformational changes in spr1814 allowing binding to the target promoter, recombinant spr1814 expressed in Escherichia coli was crystallized with the phosphoryl analogue beryllium fluoride BeF3 <sup>-</sup> by the hanging-drop vapour-diffusion method. The crystals diffracted to 1.9 Å resolution and belonged to space group P21, with unit-cell parameters a = 40.2, b = 114.5, c = 50.1 Å, β = 92.1°. Structure determination by the SAD method using the bromine derivative 5-amino-2,4,6-tribromo-isophthalic acid (B3C) is under way.

Original languageEnglish
Pages (from-to)1428-1430
Number of pages3
JournalActa Crystallographica Section F:Structural Biology Communications
Volume70
DOIs
Publication statusPublished - 2014 Oct 1

Fingerprint

streptococcus
pneumonia
Bromine
Signal transduction
Phosphorylation
regulators
Crystallization
Streptococcus pneumoniae
Aspartic Acid
X-Ray Diffraction
helices
X ray diffraction analysis
Escherichia coli
beryllium fluorides
Vapors
crystallization
analogs
Derivatives
effectors
aspartic acid

Keywords

  • Spr1814
  • Streptococcus pneumoniae

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Genetics
  • Structural Biology
  • Condensed Matter Physics

Cite this

@article{32860a7eca124b62909fe2566e3cbb68,
title = "Crystallization and preliminary X-ray diffraction analysis of full-length spr1814, a response regulator of Streptococcus pneumoniae, in complex with a phosphoryl analogue",
abstract = "Spr1814 of Streptococcus pneumoniae is a signal transduction response regulator belonging to the NarL/FixJ subfamily, which has a helix-turn-helix DNA-binding effector domain. To understand how the phosphorylation of the conserved aspartic acid residue induces conformational changes in spr1814 allowing binding to the target promoter, recombinant spr1814 expressed in Escherichia coli was crystallized with the phosphoryl analogue beryllium fluoride BeF3 - by the hanging-drop vapour-diffusion method. The crystals diffracted to 1.9 {\AA} resolution and belonged to space group P21, with unit-cell parameters a = 40.2, b = 114.5, c = 50.1 {\AA}, β = 92.1°. Structure determination by the SAD method using the bromine derivative 5-amino-2,4,6-tribromo-isophthalic acid (B3C) is under way.",
keywords = "Spr1814, Streptococcus pneumoniae",
author = "Aekyung Park and Oh, {Jae Soon} and Chi, {Young Min} and Jeong, {Seong Weon}",
year = "2014",
month = "10",
day = "1",
doi = "10.1107/S2053230X14019451",
language = "English",
volume = "70",
pages = "1428--1430",
journal = "Acta Crystallographica Section F:Structural Biology Communications",
issn = "1744-3091",
publisher = "John Wiley and Sons Ltd",

}

TY - JOUR

T1 - Crystallization and preliminary X-ray diffraction analysis of full-length spr1814, a response regulator of Streptococcus pneumoniae, in complex with a phosphoryl analogue

AU - Park, Aekyung

AU - Oh, Jae Soon

AU - Chi, Young Min

AU - Jeong, Seong Weon

PY - 2014/10/1

Y1 - 2014/10/1

N2 - Spr1814 of Streptococcus pneumoniae is a signal transduction response regulator belonging to the NarL/FixJ subfamily, which has a helix-turn-helix DNA-binding effector domain. To understand how the phosphorylation of the conserved aspartic acid residue induces conformational changes in spr1814 allowing binding to the target promoter, recombinant spr1814 expressed in Escherichia coli was crystallized with the phosphoryl analogue beryllium fluoride BeF3 - by the hanging-drop vapour-diffusion method. The crystals diffracted to 1.9 Å resolution and belonged to space group P21, with unit-cell parameters a = 40.2, b = 114.5, c = 50.1 Å, β = 92.1°. Structure determination by the SAD method using the bromine derivative 5-amino-2,4,6-tribromo-isophthalic acid (B3C) is under way.

AB - Spr1814 of Streptococcus pneumoniae is a signal transduction response regulator belonging to the NarL/FixJ subfamily, which has a helix-turn-helix DNA-binding effector domain. To understand how the phosphorylation of the conserved aspartic acid residue induces conformational changes in spr1814 allowing binding to the target promoter, recombinant spr1814 expressed in Escherichia coli was crystallized with the phosphoryl analogue beryllium fluoride BeF3 - by the hanging-drop vapour-diffusion method. The crystals diffracted to 1.9 Å resolution and belonged to space group P21, with unit-cell parameters a = 40.2, b = 114.5, c = 50.1 Å, β = 92.1°. Structure determination by the SAD method using the bromine derivative 5-amino-2,4,6-tribromo-isophthalic acid (B3C) is under way.

KW - Spr1814

KW - Streptococcus pneumoniae

UR - http://www.scopus.com/inward/record.url?scp=84927515700&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84927515700&partnerID=8YFLogxK

U2 - 10.1107/S2053230X14019451

DO - 10.1107/S2053230X14019451

M3 - Article

C2 - 25286956

AN - SCOPUS:84927515700

VL - 70

SP - 1428

EP - 1430

JO - Acta Crystallographica Section F:Structural Biology Communications

JF - Acta Crystallographica Section F:Structural Biology Communications

SN - 1744-3091

ER -