Abstract
Crystals of recombinant AbsC (subunit MW = 18 313 Da; 158 amino acids), a novel regulator of antibiotic production from Streptomyces coelicolor, were grown by vapour diffusion. The protein crystallizes in space group P2(1)2(1)2(1), with unit-cell parameters a = 43.53, b = 121.30, c = 143.75 A. Native data to a resolution of 2.25 A were recorded at station PX 14.1 (Daresbury) from a single crystal. Preliminary analysis of these data suggests that the asymmetric unit contains four copies of the AbsC monomer, giving an estimated solvent content of 47.0%. AbsC belongs to the MarR family of proteins that mediate ligand-responsive transcriptional control.
Highlights
In order to survive and compete effectively, bacteria must continuously monitor both their surroundings and their physiological status and react appropriately (Camilli & Bassler, 2006)
These cytoplasmic proteins control a variety of biological functions in bacteria, including antibiotic resistance (Miller & Sulavik, 1996; Alekshun et al, 2001), the response to oxidative stress (Spory et al, 2002; Wilkinson & Grove, 2004) and the synthesis of pathogenic factors (Rouanet et al, 2004; Wyborn et al, 2004), and they are of significant clinical interest
The structures of several MarR family members are known (Wilkinson & Grove, 2006), only the MarR structure has been determined with a bound ligand, namely salicylate (Alekshun et al, 2001), and only the OhrR structure has been determined bound to DNA (Hong et al, 2005)
Summary
In order to survive and compete effectively, bacteria must continuously monitor both their surroundings and their physiological status and react appropriately (Camilli & Bassler, 2006). The activities of the MarR family of transcriptional regulators are thought to be modulated in this way (Wilkinson & Grove, 2006) These cytoplasmic proteins control a variety of biological functions in bacteria, including antibiotic resistance (Miller & Sulavik, 1996; Alekshun et al, 2001), the response to oxidative stress (Spory et al, 2002; Wilkinson & Grove, 2004) and the synthesis of pathogenic factors (Rouanet et al, 2004; Wyborn et al, 2004), and they are of significant clinical interest. We report here the crystallization and preliminary X-ray analysis of the AbsC protein from S. coelicolor as part of a multidisciplinary study towards understanding its physiological role
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