PMID:15333946
| Citation |
Stec, E, Witkowska, M, Hryniewicz, MM, Brzozowski, AM, Wilkinson, AJ and Bujacz, GD (2004) Crystallization and preliminary crystallographic studies of the cofactor-binding domain of the LysR-type transcriptional regulator Cbl from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 60:1654-7 |
|---|---|
| Abstract |
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 C222(1), but show substantial variation of the unit-cell parameters and diffraction anisotropy. Despite this, X-ray data extending to 3.0 A resolution have been collected and solution of the structure by molecular replacement is in progress. |
| Links |
PubMed Online version:10.1107/S0907444904016841 |
| Keywords |
Adenosine Phosphosulfate/pharmacology; Bacterial Proteins/biosynthesis; Bacterial Proteins/chemistry; Bacterial Proteins/isolation & purification; Crystallization; Crystallography, X-Ray; Escherichia coli/chemistry; Escherichia coli Proteins/biosynthesis; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/isolation & purification; Protein Binding/drug effects; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Synchrotrons; Transcription Factors/biosynthesis; Transcription Factors/chemistry; Transcription Factors/isolation & purification |
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