Backbone and sidechain resonance assignments and secondary structure of Scc4 from Chlamydia trachomatis.
Backbone and sidechain resonance assignments and secondary structure of Scc4 from Chlamydia trachomatis.
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DOI：
10.1007/s12104-020-09965-4
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发表时间：
2020-10
影响因子：
0.9
通讯作者：
Macnaughtan MA
中科院分区：
文献类型：
--
作者：
Ukwaththage TO;Tonelli M;Macnaughtan MA
沙眼衣原体是一种专性细胞内细菌，可引起世界上最常见的性传播细菌性疾病。在双相发育周期中，细菌利用 III 型分泌系统 (T3SS) 作为感染性元素体侵入宿主细胞，然后分化为活跃分裂的网状体。发育周期和 T3SS 的调节通过双功能蛋白、特定的衣原体伴侣 4 (Scc4) 连接。 Scc4 是 I 类 T3SS 伴侣，与特定的衣原体伴侣 1 (Scc1) 形成异二聚体，以伴侣必需毒力效应子衣原体外膜蛋白 N (CopN)。 Scc4 还通过与 β 亚基的瓣区域和 σ66 的区域 4 之间的 RNA 聚合酶全酶结合而发挥转录因子的作用。为了研究 Scc4 双重功能背后的机制，并将其蛋白质-蛋白质相互作用作为药物开发的途径，我们正在研究 Scc4 的结构和动力学。在此过程中，我们分配了全长 Scc4 的 89.2% 主链和侧链 1H、15N 和 13C 共振。指定的化学位移用于预测二级结构和动态特性。 Scc4确定的二级结构的类型和顺序与其他细菌T3SS伴侣的X射线晶体结构一致。
Chlamydia trachomatis is an obligate intracellular bacterium that causes the most common sexually transmitted bacterial diseases in the world. With a biphasic developmental cycle, the bacteria utilize a type III secretion system (T3SS) to invade host cells as infectious elemental bodies, which then differentiate into actively dividing reticulate bodies. The regulation of the developmental cycle and the T3SS are linked by the bi-functional protein, specific Chlamydia chaperone 4 (Scc4). Scc4 is a class I T3SS chaperone forming a heterodimer with specific Chlamydia chaperone 1 (Scc1) to chaperone the essential virulence effector, Chlamydia outer membrane protein N (CopN). Scc4 also functions as a transcription factor by binding to the RNA polymerase holoenzyme between the flap region of the β subunit and region 4 of σ66. In order to investigate the mechanism behind Scc4’s dual functions and target its protein-protein interactions as a route for drug development, the structure and dynamics of Scc4 are being pursued. In the course of this effort, we assigned 89.2% of the backbone and sidechain 1H, 15N, and 13C resonances of full-length Scc4. The assigned chemical shifts were used to predict the secondary structure and dynamic properties. The type and order of Scc4’s determined secondary structure are consistent with the X-ray crystal structures of other bacterial T3SS chaperones.
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