作者: Szymon JarosÅawski , Katia Duquesne , James N. Sturgis , Simon Scheuring
DOI: 10.1111/J.1365-2958.2009.06926.X
关键词:
摘要: The outer membrane of Gram-negative bacteria protects the cell against bactericidal substances. Passage nutrients and waste is assured by porins, beta-barrel transmembrane channels. While atomic structures several porins have been solved, so far little known on supramolecular structure membrane. Here we present first high-resolution view a bacterial gently purified maintaining remnants peptidoglycan perisplasmic surface. Atomic force microscope images fragments size approximately 50% envelope revealed that are more densely packed than previously assumed. Indeed molecular sieve rather Porins cover 70% surface form locally regular lattices. potential role exposed aromatic residues in formation assembly discussed. Finally, structural data porin from marine Roseobacter denitrificans, perform sequence alignment with structure.