title: Crystal structure of chaperone protein PapD reveals an immunoglobulin fold.
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.
authors: Department of Molecular Biology, Biomedical Centre, Uppsala, Sweden.
authors: A
authors: A
authors: Holmgren
authors: C I
authors: CI
authors: Bränden
mesh_terms: D000595:Amino Acid Sequence; D000943:Antigens, Differentiation / Q000235:genetics; D001426:Bacterial Proteins; D018956:CD5 Antigens; D018833:Chaperonins; D003461:Crystallography; D004247:DNA / Q000235:genetics; D004926:Escherichia coli; D010861:Fimbriae, Bacterial; D007136:Immunoglobulins / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D011506:Proteins
chemical_list: D000943:Antigens, Differentiation; D001426:Bacterial Proteins; D018956:CD5 Antigens; D007136:Immunoglobulins; D011506:Proteins; D004247:DNA; D018833:Chaperonins