Conserved immunoglobulin-like features in a family of periplasmic pilus chaperones in bacteria.
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.
Department of Molecular Biology, Biomedical Centre, Uppsala, Sweden.
A
A
Holmgren
M J
MJ
Kuehn
C I
CI
Brändén
S J
SJ
Hultgren
D018830:Adhesins, Escherichia coli; D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000235:genetics*; D005075:Biological Evolution; D004926:Escherichia coli / Q000235:genetics*; D006193:Haemophilus influenzae / Q000235:genetics*; D006388:Hemagglutinins / Q000235:genetics*; D007136:Immunoglobulins / Q000737:chemistry / Q000235:genetics*; D007711:Klebsiella pneumoniae / Q000235:genetics*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D005810:Multigene Family; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid
D018830:Adhesins, Escherichia coli; D001425:Bacterial Outer Membrane Proteins; D006388:Hemagglutinins; D007136:Immunoglobulins