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

Authors
Park, AekyungOh, Jae SoonChi, Young MinJeong, Seong Weon
Issue Date
10월-2014
Publisher
INT UNION CRYSTALLOGRAPHY
Keywords
Spr1814; Streptococcus pneumoniae
Citation
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.70, pp.1428 - 1430
Indexed
SCOPUS
Journal Title
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume
70
Start Page
1428
End Page
1430
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/97339
DOI
10.1107/S2053230X14019451
ISSN
2053-230X
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 angstrom resolution and belonged to space group P2(1), with unit-cell parameters a = 40.2, b = 114.5, c = 50.1 angstrom, beta = 92.1 degrees. Structure determination by the SAD method using the bromine derivative 5-amino-2,4,6-tribromoisophthalic acid (B3C) is under way.
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생명과학대학 (생명공학부)
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