Structural basis for the regulation of chemotaxis by MapZ in the presence of c-di-GMP
Structural basis for the regulation of chemotaxis by MapZ in the presence of c-di-GMP
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c-di-GMP 存在下 MapZ 调节趋化性的结构基础
DOI：
10.1107/s2059798317009998
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发表时间：
2017
影响因子：
2.2
通讯作者：
Gu Lichuan
中科院分区：
文献类型：
--
作者：
Zhu Yingxiao;Yuan Zenglin;Gu Lichuan
细菌第二信使环二鸟苷酸单磷酸（c-di-GMP）通过与各种效应物结合来介导细菌生理学的多个方面。在一些情况下，这些效应物是仅含有PilZ结构域的单结构域蛋白。单结构域PilZ蛋白如何发挥功能和调节其下游靶标在很大程度上仍然未知。最近，一个单域PilZ蛋白，MapZ（PA 4608），被确定为抑制甲基转移酶CheR 1的活性。在这里，晶体结构的C-末端结构域的CheR 1含有SAH和CheR 1的复合物与c-di-GMP结合MapZ的报告。观察到MapZ在CheR 1中的结合位点与SAH/SAM结合口袋部分重叠。因此，MapZ的结合阻断SAH/SAM结合。这为在c-di-GMP存在下MapZ抑制CheR 1的机制提供了直接的结构证据。
The bacterial second messenger cyclic diguanylate monophosphate (c-di-GMP) mediates multiple aspects of bacterial physiology through binding to various effectors. In some cases, these effectors are single-domain proteins which only contain a PilZ domain. It remains largely unknown how single-domain PilZ proteins function and regulate their downstream targets. Recently, a single-domain PilZ protein, MapZ (PA4608), was identified to inhibit the activity of the methyltransferase CheR1. Here, crystal structures of the C-terminal domain of CheR1 containing SAH and of CheR1 in complex with c-di-GMP-bound MapZ are reported. It was observed that the binding site of MapZ in CheR1 partially overlaps with the SAH/SAM-binding pocket. Consequently, binding of MapZ blocks SAH/SAM binding. This provides direct structural evidence on the mechanism of inhibition of CheR1 by MapZ in the presence of c-di-GMP.