摘要
SecA is the essential component of the signal-peptide dependent translocation pathway in Escherichia coil （E.coh）. The structure and function of SecA must be known to understand the molecular mechanism of preprotein translocation. The high flexibility of SecA causes a dynamic conformational heterogeneity which presents a barrier to the growth of crystals of high diffraction quality. Electron microscopy was used to resolve the macromolecular structure of SecA in solution by negative staining and single particle analysis at a resolution of 2.9 nm. The structure of E. coil SecA is similar to the dimeric form of Bacillus subtilis SecA and is 10 nm × 10 nm × 5 nm in size.
SecA is the essential component of the signal-peptide dependent translocation pathway in Escherichia coil （E.coh）. The structure and function of SecA must be known to understand the molecular mechanism of preprotein translocation. The high flexibility of SecA causes a dynamic conformational heterogeneity which presents a barrier to the growth of crystals of high diffraction quality. Electron microscopy was used to resolve the macromolecular structure of SecA in solution by negative staining and single particle analysis at a resolution of 2.9 nm. The structure of E. coil SecA is similar to the dimeric form of Bacillus subtilis SecA and is 10 nm × 10 nm × 5 nm in size.
基金
Supported by the National Natural Science Foundation of China (Nos. 30170196 and 30330160)
