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

A. Holmgren, M. J. Kuehn, C. I. Branden, S. J. Hultgren

Research output: Contribution to journalArticle

100 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)1617-1622
Number of pages6
JournalEMBO Journal
Volume11
Issue number4
DOIs
StatePublished - Jan 1 1992

Keywords

  • Biogenesis of pili
  • Crystal structure
  • Immunoglobulin fold
  • Pathogenesis
  • Periplasmic chaperone

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