title: Crystallization and preliminary X-ray analysis of the flagellar motor `brake' molecule YcgR with c-di-GMP from Escherichia coli.
abstract: 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 Å(3) 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.
authors.affiliation: National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
authors.forename: Yanjie
authors.initials: Y
authors.lastname: Hou
authors.forename: De Feng
authors.initials: de F
authors.lastname: Li
authors.forename: Da Cheng
authors.initials: da C
authors.lastname: Wang
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D006152:Cyclic GMP / Q000031:analogs & derivatives* / Q000032:analysis / Q000737:chemistry; D004926:Escherichia coli; D029968:Escherichia coli Proteins / Q000032:analysis / Q000737:chemistry*; D005407:Flagella; D013329:Structure-Activity Relationship
chemical_list: D029968:Escherichia coli Proteins; C415947:YcgR protein, E coli; C062025:bis(3',5')-cyclic diguanylic acid; D006152:Cyclic GMP
keywords: Escherichia coli; YcgR; c-di-GMP binding protein; flagellar motility regulation