Conserved immunoglobulin-like features in a family of periplasmic pilus chaperones in bacteria.

Journal Article (Journal Article)

Detailed structural analyses revealed a family of periplasmic chaperones in Gram-negative prokaryotes which are structurally and possibly evolutionarily related to the immunoglobulin superfamily and assist in the assembly of adhesive pili. The members of this family have similar structures consistent with the overall topology of an immunoglobulin fold. Seven pilus chaperone sequences from Escherichia coli, Haemophilus influenzae and Klebsiella pneumoniae were aligned and their consensus sequence was superimposed onto the known three-dimensional structure of PapD, a representative member of the family. The molecular details of the conserved and variable structural motifs in this family of periplasmic chaperones give important insight into their structure, function, mechanism of action and evolutionary relationship with the immunoglobulin superfamily.

Full Text

Duke Authors

Cited Authors

  • Holmgren, A; Kuehn, MJ; Brändén, CI; Hultgren, SJ

Published Date

  • April 1992

Published In

Volume / Issue

  • 11 / 4

Start / End Page

  • 1617 - 1622

PubMed ID

  • 1348692

Pubmed Central ID

  • PMC556611

International Standard Serial Number (ISSN)

  • 0261-4189

Digital Object Identifier (DOI)

  • 10.1002/j.1460-2075.1992.tb05207.x


  • eng

Conference Location

  • England