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 language | English |
|---|---|
| Pages (from-to) | 1428-1430 |
| Number of pages | 3 |
| Journal | Acta Crystallographica Section F:Structural Biology Communications |
| Volume | 70 |
| DOIs | |
| Publication status | Published - 2014 Oct 1 |
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Keywords
- Spr1814
- Streptococcus pneumoniae
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Genetics
- Structural Biology
- Condensed Matter Physics
Cite this
Crystallization and preliminary X-ray diffraction analysis of full-length spr1814, a response regulator of Streptococcus pneumoniae, in complex with a phosphoryl analogue. / Park, Aekyung; Oh, Jae Soon; Chi, Young Min; Jeong, Seong Weon.
In: Acta Crystallographica Section F:Structural Biology Communications, Vol. 70, 01.10.2014, p. 1428-1430.Research output: Contribution to journal › Article
}
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 -