Crystallization and preliminary X-ray analysis of the flagellar motor ‘brake’ molecule YcgR with c-di-GMP from Escherichia coli

摘要

In Escherichia coli and Salmonella enterica, bis-(3′-5′)-cyclic dimeric guanosine monophosphate (c-di-GMP), a ubiquitous bacterial second-messenger molecule that participates in many cellular processes, can regulate flagellar motor speed and reduce cell swimming velocity by binding to the PilZ-containing protein YcgR. Here, the crystallization and preliminary X-ray crystallographic analysis of YcgR with c-di-GMP are reported. The crystals diffracted to 2.3 Å resolution and belonged to space group R3:H, with unit-cell parameters a = b = 93.96, c = 109.61 Å. The asymmetric unit appeared to contain one subunit with a Matthews coefficient of 3.21 ų Da⁻¹. The results reported here provide a sound basis for solving the crystal structure of YcgR with c-di-GMP and revealing its structure–function relationship based on the three-dimensional structure.