1ui5
From Proteopedia
Crystal structure of gamma-butyrolactone receptor (ArpA like protein)
Overview
The gamma-butyrolactone-type autoregulator/receptor systems in the Gram-positive bacterial genus Streptomyces regulate morphological differentiation or antibiotic production, or both. The autoregulator receptors act as DNA-binding proteins, and on binding their cognate ligands (gamma-butyrolactones) they are released from the DNA, thus serving as repressors. The crystal structure of CprB in Streptomyces coelicolor A3(2), a homologue of the A-factor-receptor protein, ArpA, in Streptomyces griseus, was determined. The overall structure of CprB shows that the gamma-butyrolactone receptors belong to the TetR family. CprB is composed of two domains, a DNA-binding domain and a regulatory domain. The regulatory domain contains a hydrophobic cavity, which probably serves as a ligand-binding pocket. On the basis of the crystal structure of CprB and on the analogy of the characteristics of ligand-TetR binding, the binding of gamma-butyrolactones to the regulatory domain of the receptors is supposed to induce the relocation of the DNA-binding domain through conformational changes of residues located between the ligand-binding site and the DNA-binding domain, which would result in the dissociation of the receptors from their target DNA.
About this Structure
1UI5 is a Single protein structure of sequence from Streptomyces coelicolor. Full crystallographic information is available from OCA.
Reference
Crystal structure of a gamma-butyrolactone autoregulator receptor protein in Streptomyces coelicolor A3(2)., Natsume R, Ohnishi Y, Senda T, Horinouchi S, J Mol Biol. 2004 Feb 13;336(2):409-19. PMID:14757054 Page seeded by OCA on Sat May 3 11:15:47 2008
