Crystal structure of a γ-butyrolactone autoregulator receptor protein in Streptomyces coelicolor A3(2)
Crystal structure of a γ-butyrolactone autoregulator receptor protein in Streptomyces coelicolor A3(2)
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DOI：
10.1016/j.jmb.2003.12.040
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发表时间：
2004-02-13
影响因子：
5.6
通讯作者：
Horinouchi, S
中科院分区：
文献类型：
--
作者：
Natsume, R;Ohnishi, Y;Horinouchi, S
革兰氏阳性细菌链霉菌属中的γ-丁内酯型自动调节子/受体系统调节形态分化或抗生素产生，或两者。自动调节受体作为DNA结合蛋白，在结合其同源配体（γ-丁内酯）时，它们从DNA中释放出来，从而作为阻遏物。天蓝色链霉菌A3（2）中CprB的晶体结构已确定，它是灰色链霉菌中A因子受体蛋白ArpA的同源物。CprB的整体结构表明γ-丁内酯受体属于TetR家族。CprB由两个结构域组成，DNA结合结构域和调节结构域。调控域包含一个疏水腔，可能作为一个配体结合口袋。根据CprB的晶体结构和TetR与配体结合的相似性，推测γ-丁内酯与受体调节结构域的结合是通过改变配体结合位点和DNA结合结构域之间的残基的构象而引起DNA结合结构域的重新定位，从而导致受体与靶DNA的解离。(C)2003 Elsevier Ltd.保留所有权利。
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. (C) 2003 Elsevier Ltd. All rights reserved.