Open AccessCrystallization and preliminary X‐ray studies of SdiA from Escherichia coli
Author(s) -
Wu Chunai,
Lokanath Neratur K.,
Kim Dong Young,
Nguyen Lan Dao Ngoc,
Kim Kyeong Kyu
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107059696
Subject(s) - operon , quorum sensing , escherichia coli , nucleoid , recombinant dna , chemistry , microbiology and biotechnology , crystallography , bacteria , biology , gene , genetics , biochemistry , biofilm
SdiA enhances cell division by regulating the fts QAZ operon in Escherichia coli as a transcription activator. In addition, SdiA is suggested to play a role in detecting quorum signals that emanate from other species. It is therefore a homologue of LuxR, a cognate quorum‐sensing receptor that recognizes a quorum signal and activates the quorum responses. To elucidate the role of SdiA and its functional and structural relationship to LuxR, structural studies were performed on E. coli SdiA. Recombinant SdiA was overexpressed, purified and crystallized at 287 K using the hanging‐drop vapour‐diffusion method. X‐ray diffraction data from a native crystal were collected with 99.7% completeness to 2.7 Å resolution with an R merge of 6.0%. The crystals belong to the hexagonal space group P 6 1 22 or P 6 5 22, with unit‐cell parameters a = b = 130.47, c = 125.23 Å.