3zmd | pdb_00003zmd

Crystal structure of AbsC, a MarR family transcriptional regulator from Streptomyces coelicolor

spinqualitylabelsall models 3zmd, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3zmd is a 4 chain structure with sequence from "actinomyces_coelicolor"_(muller_1908)_lieske_1921 "actinomyces coelicolor" (muller 1908) lieske 1921. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, EDO, NA, SAL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Crystallization and preliminary X-ray analysis of AbsC, a novel regulator of antibiotic production in Streptomyces coelicolor.,Stevenson CE, Kock H, Mootien S, Davies SC, Bibb MJ, Lawson DM Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Mar 1;63(Pt 3):233-5. Epub, 2007 Feb 23. PMID:17329821 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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