5 years ago

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
Lichuan Gu, Zenglin Yuan, Yingxiao Zhu
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.The structure of CheR1 in complex with c-di-GMP-bound MapZ is reported and the complex biochemical process which involves CheR1, MapZ, SAH/SAM and c-di-GMP is revealed.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1107/S2059798317009998

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