PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbA (original) (raw)

Abstract

Adhesive P pili of uropathogenic Escherichia coli were not assembled by a strain that lacks the periplasmic dulfide isomerase DsbA. This defect was mostly attributed to the immunoglobulin-like pilus chaperone PapD, which possesses an unusual Intrasheet disulfide bond between the last two (.strands of its CD4-like carboxyl-terminal domain. The

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