PMID:10698927

Citation	No author listed (2000) SecYEG assembles into a tetramer to form the active protein translocation channel. EMBO J. 19:852-61
Abstract	Translocase mediates preprotein translocation across the Escherichia coli inner membrane. It consists of the SecYEG integral membrane protein complex and the peripheral ATPase SecA. Here we show by functional assays, negative-stain electron microscopy and mass measurements with the scanning transmission microscope that SecA recruits SecYEG complexes to form the active translocation channel. The active assembly of SecYEG has a side length of 10.5 nm and exhibits an approximately 5 nm central cavity. The mass and structure of this SecYEG as well as the subunit stoichiometry of SecA and SecY in a soluble translocase-precursor complex reveal that translocase consists of the SecA homodimer and four SecYEG complexes.
Links	PubMed PMC305625 Online version:10.1093/emboj/19.5.852
Keywords	Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Biological Transport; Cell Membrane/metabolism; Dimerization; Escherichia coli; Escherichia coli Proteins; Mass Spectrometry; Membrane Proteins/chemistry; Membrane Proteins/metabolism; Protein Binding
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Gene product	Qualifier	GO ID	GO term name	Evidence Code	with/from	Aspect	Notes	Status
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