Open AccessCrystallization and preliminary crystallographic studies of the cofactor‐binding domain of the LysR‐type transcriptional regulator Cbl from Escherichia coli
Author(s) -
Stec Emilia,
Witkowska Malgorzata,
Hryniewicz Monika M.,
Brzozowski Andrzej M.,
Wilkinson Anthony J.,
Bujacz Grzegorz D.
Publication year - 2004
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444904016841
Subject(s) - escherichia coli , transcriptional regulation , cofactor , transcription factor , inducer , gene , transcription (linguistics) , biology , chemistry , regulator , biochemistry , crystallography , enzyme , linguistics , philosophy
Cbl (CysB‐like protein) is a member of the family of LysR‐type transcriptional regulators (LTTRs) and controls genes engaged in sulfur assimilation in Escherichia coli . It has been postulated that adenosine 5‐phosphosulfate (APS) is responsible for abolishing Cbl‐activated transcription from the ssu promoter (Bykowski et al. , 2002). To elucidate the structural basis of Cbl function and to confirm the role of APS as an anti‐inducer, the cofactor‐binding domain of Cbl (c‐Cbl, MW = 26 kDa) was cloned, purified and crystallized in the presence of APS. The crystals belong to space group C 222 1 , but show substantial variation of the unit‐cell parameters and diffraction anisotropy. Despite this, X‐ray data extending to 3.0 Å resolution have been collected and solution of the structure by molecular replacement is in progress.