title: Solution structure of the bacterial chemotaxis adaptor protein CheW from Escherichia coli.
abstract: The bacterial chemotaxis adaptor protein CheW physically links the chemoreceptors (MCPs) and the histidine kinase CheA. Extensive investigations using bacterium Escherichia coli have established the central role of CheW in the MCP-modulated activation of CheA. Here we report the solution structure of CheW from E. coli determined by NMR spectroscopy. The results show that E. coli CheW shares an overall fold with previously reported structure of CheW from Thermotoga maritima, whereas local conformational deviations are observed. In particular, the C-terminal alpha-helix is considerably longer in E. coli CheW and appears to shrink the active binding pocket with CheA. Our study provides the structural basis for further investigations in E. coli chemotaxis.
authors.affiliation: Beijing Nuclear Magnetic Resonance Center, Peking University, Beijing 100871, China.
authors.forename: You
authors.initials: Y
authors.lastname: Li
authors.forename: Yunfei
authors.initials: Y
authors.lastname: Hu
authors.forename: Wenyu
authors.initials: W
authors.lastname: Fu
authors.forename: Bin
authors.initials: B
authors.lastname: Xia
authors.forename: Changwen
authors.initials: C
authors.lastname: Jin
mesh_terms: D004926:Escherichia coli / Q000737:chemistry*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation
chemical_list: C489103:CheW protein, E coli; D029968:Escherichia coli Proteins