Crystal structure of chaperone protein PapD reveals an immunoglobulin fold

Nature. 1989 Nov 16;342(6247):248-51. doi: 10.1038/342248a0.

Abstract

The chaperone protein PapD mediates assembly of pili in Escherichia coli. Its polypeptide chain folds into two immunoglobulin-type domains that are homologous in sequence to the human lymphocyte differentiation antigen Leu-1/CD5.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Antigens, Differentiation / genetics
  • Bacterial Proteins*
  • CD5 Antigens
  • Chaperonins
  • Crystallography
  • DNA / genetics
  • Escherichia coli
  • Fimbriae, Bacterial
  • Immunoglobulins / genetics
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Processing, Post-Translational
  • Proteins*

Substances

  • Antigens, Differentiation
  • Bacterial Proteins
  • CD5 Antigens
  • Immunoglobulins
  • Proteins
  • DNA
  • Chaperonins