Structural basis of chaperone self-capping in P pilus biogenesis

D. L. Hung, J. S. Pinkner, S. D. Knight, S. J. Hultgren

Research output: Contribution to journalArticlepeer-review

28 Scopus citations


PapD is an immunoglobulin-like chaperone that mediates the assembly of P pill in uropathogenic strains of Escherichia coli. It binds and caps interactive surfaces on pilus subunits to prevent their premature associations in the periplasm. We elucidated the structural basis of a mechanism whereby PapD also interacts with itself, capping its own subunit binding surface. Crystal structures of dimeric forms of PapD revealed that this self-capping mechanism involves a rearrangement and ordering of the C2- D2 and F1-G1 loops upon dimerization which might ensure that a stable dimer is not formed in solution in spite of a relatively large dimer interface. An analysis of site directed mutations revealed that chaperone dimerization requires the same surface that is otherwise used to bind subunits.

Original languageEnglish
Pages (from-to)8178-8183
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number14
StatePublished - Jul 6 1999


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