期刊
SCIENCE
卷 320, 期 5874, 页码 376-379出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1154994
关键词
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Type 1 pili from uropathogenic Escherichia coli are a prototype of adhesive surface organelles assembled and secreted by the conserved chaperone/ usher pathway. We reconstituted type 1 pilus biogenesis from purified pilus proteins. The usher FimD acted as a catalyst to accelerate the ordered assembly of protein subunits independently of cellular energy. Its activity was highly dependent on the adhesin subunit FimH, which triggered the conversion of FimD into a high-efficiency assembly catalyst. Furthermore, a simple kinetic model adequately rationalized usher- catalyzed pilus assembly in vivo. Our results contribute to a mechanistic understanding of protein- catalyzed biogenesis of supramolecular protein complexes at the bacterial outer cell membrane.
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